[{"article_type":"original","publisher":"ACS","language":[{"iso":"eng"}],"page":"7952-7957","quality_controlled":"1","title":"Li–O2 battery with a dimethylformamide electrolyte","month":"04","intvolume":"       134","publication_status":"published","oa_version":"None","date_created":"2020-01-15T12:19:36Z","article_processing_charge":"No","author":[{"full_name":"Chen, Yuhui","last_name":"Chen","first_name":"Yuhui"},{"full_name":"Freunberger, Stefan Alexander","orcid":"0000-0003-2902-5319","last_name":"Freunberger","first_name":"Stefan Alexander","id":"A8CA28E6-CE23-11E9-AD2D-EC27E6697425"},{"first_name":"Zhangquan","last_name":"Peng","full_name":"Peng, Zhangquan"},{"first_name":"Fanny","last_name":"Bardé","full_name":"Bardé, Fanny"},{"full_name":"Bruce, Peter G.","last_name":"Bruce","first_name":"Peter G."}],"issue":"18","_id":"7311","publication":"Journal of the American Chemical Society","extern":"1","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","volume":134,"abstract":[{"lang":"eng","text":"Stability of the electrolyte toward reduced oxygen species generated at the cathode is a crucial challenge for the rechargeable nonaqueous Li–O2 battery. Here, we investigate dimethylformamide as the basis of an electrolyte. Although reactions at the O2 cathode on the first discharge–charge cycle are dominated by reversible Li2O2 formation/decomposition, there is also electrolyte decomposition, which increases on cycling. The products of decomposition at the cathode on discharge are Li2O2, Li2CO3, HCO2Li, CH3CO2Li, NO, H2O, and CO2. Li2CO3 accumulates in the electrode with cycling. The stability of dimethylformamide toward reduced oxygen species is insufficient for its use in the rechargeable nonaqueous Li–O2 battery."}],"doi":"10.1021/ja302178w","publication_identifier":{"issn":["0002-7863","1520-5126"]},"day":"19","date_published":"2012-04-19T00:00:00Z","type":"journal_article","date_updated":"2021-01-12T08:12:58Z","year":"2012","citation":{"mla":"Chen, Yuhui, et al. “Li–O2 Battery with a Dimethylformamide Electrolyte.” <i>Journal of the American Chemical Society</i>, vol. 134, no. 18, ACS, 2012, pp. 7952–57, doi:<a href=\"https://doi.org/10.1021/ja302178w\">10.1021/ja302178w</a>.","short":"Y. Chen, S.A. Freunberger, Z. Peng, F. Bardé, P.G. Bruce, Journal of the American Chemical Society 134 (2012) 7952–7957.","ista":"Chen Y, Freunberger SA, Peng Z, Bardé F, Bruce PG. 2012. Li–O2 battery with a dimethylformamide electrolyte. Journal of the American Chemical Society. 134(18), 7952–7957.","ama":"Chen Y, Freunberger SA, Peng Z, Bardé F, Bruce PG. Li–O2 battery with a dimethylformamide electrolyte. <i>Journal of the American Chemical Society</i>. 2012;134(18):7952-7957. doi:<a href=\"https://doi.org/10.1021/ja302178w\">10.1021/ja302178w</a>","apa":"Chen, Y., Freunberger, S. A., Peng, Z., Bardé, F., &#38; Bruce, P. G. (2012). Li–O2 battery with a dimethylformamide electrolyte. <i>Journal of the American Chemical Society</i>. ACS. <a href=\"https://doi.org/10.1021/ja302178w\">https://doi.org/10.1021/ja302178w</a>","ieee":"Y. Chen, S. A. Freunberger, Z. Peng, F. Bardé, and P. G. Bruce, “Li–O2 battery with a dimethylformamide electrolyte,” <i>Journal of the American Chemical Society</i>, vol. 134, no. 18. ACS, pp. 7952–7957, 2012.","chicago":"Chen, Yuhui, Stefan Alexander Freunberger, Zhangquan Peng, Fanny Bardé, and Peter G. Bruce. “Li–O2 Battery with a Dimethylformamide Electrolyte.” <i>Journal of the American Chemical Society</i>. ACS, 2012. <a href=\"https://doi.org/10.1021/ja302178w\">https://doi.org/10.1021/ja302178w</a>."}},{"author":[{"full_name":"Chovnik, Olga","first_name":"Olga","last_name":"Chovnik"},{"last_name":"Balgley","first_name":"Renata","full_name":"Balgley, Renata"},{"first_name":"Joel R.","last_name":"Goldman","full_name":"Goldman, Joel R."},{"full_name":"Klajn, Rafal","last_name":"Klajn","first_name":"Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"}],"issue":"48","_id":"13407","pmid":1,"scopus_import":"1","title":"Dynamically self-assembling carriers enable guiding of diamagnetic particles by weak magnets","intvolume":"       134","publication_status":"published","date_created":"2023-08-01T09:47:42Z","article_processing_charge":"No","page":"19564-19567","quality_controlled":"1","article_type":"original","publisher":"American Chemical Society","external_id":{"pmid":["23181449"]},"date_updated":"2023-08-08T07:51:10Z","year":"2012","citation":{"chicago":"Chovnik, Olga, Renata Balgley, Joel R. Goldman, and Rafal Klajn. “Dynamically Self-Assembling Carriers Enable Guiding of Diamagnetic Particles by Weak Magnets.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2012. <a href=\"https://doi.org/10.1021/ja309633v\">https://doi.org/10.1021/ja309633v</a>.","ieee":"O. Chovnik, R. Balgley, J. R. Goldman, and R. Klajn, “Dynamically self-assembling carriers enable guiding of diamagnetic particles by weak magnets,” <i>Journal of the American Chemical Society</i>, vol. 134, no. 48. American Chemical Society, pp. 19564–19567, 2012.","ama":"Chovnik O, Balgley R, Goldman JR, Klajn R. Dynamically self-assembling carriers enable guiding of diamagnetic particles by weak magnets. <i>Journal of the American Chemical Society</i>. 2012;134(48):19564-19567. doi:<a href=\"https://doi.org/10.1021/ja309633v\">10.1021/ja309633v</a>","apa":"Chovnik, O., Balgley, R., Goldman, J. R., &#38; Klajn, R. (2012). Dynamically self-assembling carriers enable guiding of diamagnetic particles by weak magnets. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja309633v\">https://doi.org/10.1021/ja309633v</a>","ista":"Chovnik O, Balgley R, Goldman JR, Klajn R. 2012. Dynamically self-assembling carriers enable guiding of diamagnetic particles by weak magnets. Journal of the American Chemical Society. 134(48), 19564–19567.","mla":"Chovnik, Olga, et al. “Dynamically Self-Assembling Carriers Enable Guiding of Diamagnetic Particles by Weak Magnets.” <i>Journal of the American Chemical Society</i>, vol. 134, no. 48, American Chemical Society, 2012, pp. 19564–67, doi:<a href=\"https://doi.org/10.1021/ja309633v\">10.1021/ja309633v</a>.","short":"O. Chovnik, R. Balgley, J.R. Goldman, R. Klajn, Journal of the American Chemical Society 134 (2012) 19564–19567."},"abstract":[{"lang":"eng","text":"We show that diamagnetic particles can be remotely manipulated by a magnet by the reversible adsorption of dual-responsive, light-switchable/superparamagnetic nanoparticles down to their surface. Adsorption occurs upon exposure to UV light, and can be reversed thermally or by ambient light. The dynamic self-assembly of thin films of the dual-responsive nanoparticles induces attractive interactions between diamagnetic particles. We demonstrate that catalytic amounts of the dual-responsive nanoparticles are sufficient to magnetically guide and deliver the diamagnetic particles to desired locations, where they can then be released by disassembling the dynamic layers of superparamagnetic nanoparticles with visible light."}],"doi":"10.1021/ja309633v","day":"26","extern":"1","volume":134,"publication":"Journal of the American Chemical Society","month":"11","oa_version":"Published Version","language":[{"iso":"eng"}],"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"date_published":"2012-11-26T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87"},{"volume":133,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","extern":"1","year":"2011","citation":{"ieee":"S. A. Freunberger <i>et al.</i>, “Reactions in the rechargeable Lithium–O2 battery with alkyl carbonate electrolytes,” <i>Journal of the American Chemical Society</i>, vol. 133, no. 20. ACS, pp. 8040–8047, 2011.","chicago":"Freunberger, Stefan Alexander, Yuhui Chen, Zhangquan Peng, John M. Griffin, Laurence J. Hardwick, Fanny Bardé, Petr Novák, and Peter G. Bruce. “Reactions in the Rechargeable Lithium–O2 Battery with Alkyl Carbonate Electrolytes.” <i>Journal of the American Chemical Society</i>. ACS, 2011. <a href=\"https://doi.org/10.1021/ja2021747\">https://doi.org/10.1021/ja2021747</a>.","ama":"Freunberger SA, Chen Y, Peng Z, et al. Reactions in the rechargeable Lithium–O2 battery with alkyl carbonate electrolytes. <i>Journal of the American Chemical Society</i>. 2011;133(20):8040-8047. doi:<a href=\"https://doi.org/10.1021/ja2021747\">10.1021/ja2021747</a>","apa":"Freunberger, S. A., Chen, Y., Peng, Z., Griffin, J. M., Hardwick, L. J., Bardé, F., … Bruce, P. G. (2011). Reactions in the rechargeable Lithium–O2 battery with alkyl carbonate electrolytes. <i>Journal of the American Chemical Society</i>. ACS. <a href=\"https://doi.org/10.1021/ja2021747\">https://doi.org/10.1021/ja2021747</a>","ista":"Freunberger SA, Chen Y, Peng Z, Griffin JM, Hardwick LJ, Bardé F, Novák P, Bruce PG. 2011. Reactions in the rechargeable Lithium–O2 battery with alkyl carbonate electrolytes. Journal of the American Chemical Society. 133(20), 8040–8047.","short":"S.A. Freunberger, Y. Chen, Z. Peng, J.M. Griffin, L.J. Hardwick, F. Bardé, P. Novák, P.G. Bruce, Journal of the American Chemical Society 133 (2011) 8040–8047.","mla":"Freunberger, Stefan Alexander, et al. “Reactions in the Rechargeable Lithium–O2 Battery with Alkyl Carbonate Electrolytes.” <i>Journal of the American Chemical Society</i>, vol. 133, no. 20, ACS, 2011, pp. 8040–47, doi:<a href=\"https://doi.org/10.1021/ja2021747\">10.1021/ja2021747</a>."},"date_updated":"2021-01-12T08:13:00Z","type":"journal_article","date_published":"2011-04-27T00:00:00Z","publication_identifier":{"issn":["0002-7863","1520-5126"]},"day":"27","doi":"10.1021/ja2021747","abstract":[{"text":"The nonaqueous rechargeable lithium–O2 battery containing an alkyl carbonate electrolyte discharges by formation of C3H6(OCO2Li)2, Li2CO3, HCO2Li, CH3CO2Li, CO2, and H2O at the cathode, due to electrolyte decomposition. Charging involves oxidation of C3H6(OCO2Li)2, Li2CO3, HCO2Li, CH3CO2Li accompanied by CO2 and H2O evolution. Mechanisms are proposed for the reactions on discharge and charge. The different pathways for discharge and charge are consistent with the widely observed voltage gap in Li–O2 cells. Oxidation of C3H6(OCO2Li)2 involves terminal carbonate groups leaving behind the OC3H6O moiety that reacts to form a thick gel on the Li anode. Li2CO3, HCO2Li, CH3CO2Li, and C3H6(OCO2Li)2 accumulate in the cathode on cycling correlating with capacity fading and cell failure. The latter is compounded by continuous consumption of the electrolyte on each discharge.","lang":"eng"}],"quality_controlled":"1","page":"8040-8047","language":[{"iso":"eng"}],"publisher":"ACS","article_type":"original","_id":"7316","publication":"Journal of the American Chemical Society","issue":"20","author":[{"id":"A8CA28E6-CE23-11E9-AD2D-EC27E6697425","first_name":"Stefan Alexander","last_name":"Freunberger","orcid":"0000-0003-2902-5319","full_name":"Freunberger, Stefan Alexander"},{"full_name":"Chen, Yuhui","last_name":"Chen","first_name":"Yuhui"},{"first_name":"Zhangquan","last_name":"Peng","full_name":"Peng, Zhangquan"},{"last_name":"Griffin","first_name":"John M.","full_name":"Griffin, John M."},{"full_name":"Hardwick, Laurence J.","first_name":"Laurence J.","last_name":"Hardwick"},{"first_name":"Fanny","last_name":"Bardé","full_name":"Bardé, Fanny"},{"first_name":"Petr","last_name":"Novák","full_name":"Novák, Petr"},{"full_name":"Bruce, Peter G.","last_name":"Bruce","first_name":"Peter G."}],"article_processing_charge":"No","date_created":"2020-01-15T12:20:43Z","oa_version":"None","publication_status":"published","intvolume":"       133","month":"04","title":"Reactions in the rechargeable Lithium–O2 battery with alkyl carbonate electrolytes"},{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","extern":"1","volume":132,"abstract":[{"lang":"eng","text":"Characterization of protein dynamics by solid-state NMR spectroscopy requires robust and accurate measurement protocols, which are not yet fully developed. In this study, we investigate the backbone dynamics of microcrystalline ubiquitin using different approaches. A rotational-echo double-resonance type (REDOR-type) methodology allows one to accurately measure 1H−15N order parameters in highly deuterated samples. We show that the systematic errors in the REDOR experiment are as low as 1% or even less, giving access to accurate data for the amplitudes of backbone mobility. Combining such dipolar-coupling-derived order parameters with autocorrelated and cross-correlated 15N relaxation rates, we are able to quantitate amplitudes and correlation times of backbone dynamics on picosecond and nanosecond time scales in a residue-resolved manner. While the mobility on picosecond time scales appears to have rather uniform amplitude throughout the protein, we unambiguously identify and quantitate nanosecond mobility with order parameters S2 as low as 0.8 in some regions of the protein, where nanosecond dynamics has also been revealed in solution state. The methodology used here, a combination of accurate dipolar-coupling measurements and different relaxation parameters, yields details about dynamics on different time scales and can be applied to solid protein samples such as amyloid fibrils or membrane proteins."}],"publication_identifier":{"issn":["0002-7863","1520-5126"]},"day":"26","doi":"10.1021/ja100726a","type":"journal_article","date_published":"2010-10-26T00:00:00Z","citation":{"short":"P. Schanda, B.H. Meier, M. Ernst, Journal of the American Chemical Society 132 (2010) 15957–15967.","mla":"Schanda, Paul, et al. “Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.” <i>Journal of the American Chemical Society</i>, vol. 132, no. 45, American Chemical Society, 2010, pp. 15957–67, doi:<a href=\"https://doi.org/10.1021/ja100726a\">10.1021/ja100726a</a>.","ista":"Schanda P, Meier BH, Ernst M. 2010. Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. Journal of the American Chemical Society. 132(45), 15957–15967.","ama":"Schanda P, Meier BH, Ernst M. Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. <i>Journal of the American Chemical Society</i>. 2010;132(45):15957-15967. doi:<a href=\"https://doi.org/10.1021/ja100726a\">10.1021/ja100726a</a>","apa":"Schanda, P., Meier, B. H., &#38; Ernst, M. (2010). Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja100726a\">https://doi.org/10.1021/ja100726a</a>","chicago":"Schanda, Paul, Beat H. Meier, and Matthias Ernst. “Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2010. <a href=\"https://doi.org/10.1021/ja100726a\">https://doi.org/10.1021/ja100726a</a>.","ieee":"P. Schanda, B. H. Meier, and M. Ernst, “Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy,” <i>Journal of the American Chemical Society</i>, vol. 132, no. 45. American Chemical Society, pp. 15957–15967, 2010."},"year":"2010","date_updated":"2021-01-12T08:19:30Z","article_type":"original","publisher":"American Chemical Society","language":[{"iso":"eng"}],"quality_controlled":"1","page":"15957-15967","intvolume":"       132","month":"10","title":"Quantitative analysis of protein backbone dynamics in microcrystalline ubiquitin by solid-state NMR spectroscopy","article_processing_charge":"No","date_created":"2020-09-18T10:11:13Z","oa_version":"None","publication_status":"published","issue":"45","author":[{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul"},{"full_name":"Meier, Beat H.","last_name":"Meier","first_name":"Beat H."},{"full_name":"Ernst, Matthias","last_name":"Ernst","first_name":"Matthias"}],"_id":"8472","publication":"Journal of the American Chemical Society"},{"external_id":{"pmid":["20218598"]},"date_updated":"2023-08-08T08:00:31Z","year":"2010","citation":{"ista":"Coskun A, Wesson PJ, Klajn R, Trabolsi A, Fang L, Olson MA, Dey SK, Grzybowski BA, Stoddart JF. 2010. Molecular-mechanical switching at the nanoparticle−solvent interface: Practice and theory. Journal of the American Chemical Society. 132(12), 4310–4320.","short":"A. Coskun, P.J. Wesson, R. Klajn, A. Trabolsi, L. Fang, M.A. Olson, S.K. Dey, B.A. Grzybowski, J.F. Stoddart, Journal of the American Chemical Society 132 (2010) 4310–4320.","mla":"Coskun, Ali, et al. “Molecular-Mechanical Switching at the Nanoparticle−solvent Interface: Practice and Theory.” <i>Journal of the American Chemical Society</i>, vol. 132, no. 12, American Chemical Society, 2010, pp. 4310–20, doi:<a href=\"https://doi.org/10.1021/ja9102327\">10.1021/ja9102327</a>.","chicago":"Coskun, Ali, Paul J. Wesson, Rafal Klajn, Ali Trabolsi, Lei Fang, Mark A. Olson, Sanjeev K. Dey, Bartosz A. Grzybowski, and J. Fraser Stoddart. “Molecular-Mechanical Switching at the Nanoparticle−solvent Interface: Practice and Theory.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2010. <a href=\"https://doi.org/10.1021/ja9102327\">https://doi.org/10.1021/ja9102327</a>.","ieee":"A. Coskun <i>et al.</i>, “Molecular-mechanical switching at the nanoparticle−solvent interface: Practice and theory,” <i>Journal of the American Chemical Society</i>, vol. 132, no. 12. American Chemical Society, pp. 4310–4320, 2010.","ama":"Coskun A, Wesson PJ, Klajn R, et al. Molecular-mechanical switching at the nanoparticle−solvent interface: Practice and theory. <i>Journal of the American Chemical Society</i>. 2010;132(12):4310-4320. doi:<a href=\"https://doi.org/10.1021/ja9102327\">10.1021/ja9102327</a>","apa":"Coskun, A., Wesson, P. J., Klajn, R., Trabolsi, A., Fang, L., Olson, M. A., … Stoddart, J. F. (2010). Molecular-mechanical switching at the nanoparticle−solvent interface: Practice and theory. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja9102327\">https://doi.org/10.1021/ja9102327</a>"},"abstract":[{"lang":"eng","text":"A range (Au, Pt, Pd) of metal nanoparticles (MNPs) has been prepared and functionalized with (a) redox-active stalks containing tetrathiafulvalene (TTF) units, (b) [2]pseudorotaxanes formed between these stalks and cyclobis(paraquat-p-phenylene) (CBPQT4+) rings, and (c) bistable [2]rotaxane molecules where the dumbbell component contains a 1,5-dioxynaphthalene (DNP) unit, as well as a TTF unit, encircled by a CBPQT4+ ring. It transpires that the molecules present in (a) and (c) and the supermolecules described in (b) retain their switching characteristics, previously observed in solution, when they are immobilized onto MNPs. Moreover, their oxidation potentials depend on the fraction, χ, of the molecules or supermolecules on the surface of the nanoparticles. A variation in χ affects the oxidation potentials of the TTF units to the extent that switching can be subjected to fine tuning as a result. Specifically, increasing χ results in positive shifts (i) in the oxidation potentials of the TTF unit in (a)−(c) and (ii) the reduction potentials of the CBPQT4+ rings in (c). These shifts can be attributed to an increase in the electrostatic potential surrounding the MNPs. Both the magnitude and the direction of these shifts are reproduced by a model, based on the Poisson−Boltzmann equation coupled with charge-regulating boundary conditions. Furthermore, the kinetics of relaxation from the metastable state coconformation (MSCC) to the ground-state coconformation (GSCC) of the bistable [2]rotaxane molecules also depends on χ, as well as on the nanoparticle diameter. Increasing either of these parameters accelerates the rate of relaxation from the MSCC to the GSCC. This rate is a function of (i) the activation energy for the relaxation process associated with the bistable [2]rotaxane molecules in solution and (ii) the electrostatic potential surrounding the MNPs. The electrostatic potential depends on (i) the diameter of the MNPs, (ii) the amount of the bistable [2]rotaxane molecules on the surface of the MNPs, and (iii) the equilibrium distribution of the CBPQT4+ rings between the DNP and TTF recognition sites in the GSCC. This electrostatic potential has also been quantified using the Poisson−Boltzmann equation, leading to faithful estimates of the rate constants."}],"doi":"10.1021/ja9102327","day":"31","extern":"1","volume":132,"author":[{"first_name":"Ali","last_name":"Coskun","full_name":"Coskun, Ali"},{"last_name":"Wesson","first_name":"Paul J.","full_name":"Wesson, Paul J."},{"id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b","last_name":"Klajn","first_name":"Rafal","full_name":"Klajn, Rafal"},{"last_name":"Trabolsi","first_name":"Ali","full_name":"Trabolsi, Ali"},{"first_name":"Lei","last_name":"Fang","full_name":"Fang, Lei"},{"last_name":"Olson","first_name":"Mark A.","full_name":"Olson, Mark A."},{"last_name":"Dey","first_name":"Sanjeev K.","full_name":"Dey, Sanjeev K."},{"full_name":"Grzybowski, Bartosz A.","first_name":"Bartosz A.","last_name":"Grzybowski"},{"full_name":"Stoddart, J. Fraser","first_name":"J. Fraser","last_name":"Stoddart"}],"issue":"12","pmid":1,"_id":"13410","scopus_import":"1","title":"Molecular-mechanical switching at the nanoparticle−solvent interface: Practice and theory","intvolume":"       132","publication_status":"published","article_processing_charge":"No","date_created":"2023-08-01T09:48:27Z","page":"4310-4320","quality_controlled":"1","article_type":"original","publisher":"American Chemical Society","date_published":"2010-03-31T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","publication":"Journal of the American Chemical Society","month":"03","oa_version":"None","language":[{"iso":"eng"}],"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"]},{"date_published":"2009-06-01T00:00:00Z","type":"journal_article","date_updated":"2021-01-12T08:19:32Z","year":"2009","citation":{"ista":"Farjon J, Boisbouvier J, Schanda P, Pardi A, Simorre J-P, Brutscher B. 2009. Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. Journal of the American Chemical Society. 131(24), 8571–8577.","short":"J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, B. Brutscher, Journal of the American Chemical Society 131 (2009) 8571–8577.","mla":"Farjon, Jonathan, et al. “Longitudinal-Relaxation-Enhanced NMR Experiments for the Study of Nucleic Acids in Solution.” <i>Journal of the American Chemical Society</i>, vol. 131, no. 24, American Chemical Society, 2009, pp. 8571–77, doi:<a href=\"https://doi.org/10.1021/ja901633y\">10.1021/ja901633y</a>.","ieee":"J. Farjon, J. Boisbouvier, P. Schanda, A. Pardi, J.-P. Simorre, and B. Brutscher, “Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution,” <i>Journal of the American Chemical Society</i>, vol. 131, no. 24. American Chemical Society, pp. 8571–8577, 2009.","chicago":"Farjon, Jonathan, Jérôme Boisbouvier, Paul Schanda, Arthur Pardi, Jean-Pierre Simorre, and Bernhard Brutscher. “Longitudinal-Relaxation-Enhanced NMR Experiments for the Study of Nucleic Acids in Solution.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2009. <a href=\"https://doi.org/10.1021/ja901633y\">https://doi.org/10.1021/ja901633y</a>.","apa":"Farjon, J., Boisbouvier, J., Schanda, P., Pardi, A., Simorre, J.-P., &#38; Brutscher, B. (2009). Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja901633y\">https://doi.org/10.1021/ja901633y</a>","ama":"Farjon J, Boisbouvier J, Schanda P, Pardi A, Simorre J-P, Brutscher B. Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution. <i>Journal of the American Chemical Society</i>. 2009;131(24):8571-8577. doi:<a href=\"https://doi.org/10.1021/ja901633y\">10.1021/ja901633y</a>"},"abstract":[{"lang":"eng","text":"Atomic-resolution information on the structure and dynamics of nucleic acids is essential for a better understanding of the mechanistic basis of many cellular processes. NMR spectroscopy is a powerful method for studying the structure and dynamics of nucleic acids; however, solution NMR studies are currently limited to relatively small nucleic acids at high concentrations. Thus, technological and methodological improvements that increase the experimental sensitivity and spectral resolution of NMR spectroscopy are required for studies of larger nucleic acids or protein−nucleic acid complexes. Here we introduce a series of imino-proton-detected NMR experiments that yield an over 2-fold increase in sensitivity compared to conventional pulse schemes. These methods can be applied to the detection of base pair interactions, RNA−ligand titration experiments, measurement of residual dipolar 15N−1H couplings, and direct measurements of conformational transitions. These NMR experiments employ longitudinal spin relaxation enhancement techniques that have proven useful in protein NMR spectroscopy. The performance of these new experiments is demonstrated for a 10 kDa TAR-TAR*GA RNA kissing complex and a 26 kDa tRNA."}],"doi":"10.1021/ja901633y","publication_identifier":{"issn":["0002-7863","1520-5126"]},"day":"01","extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","volume":131,"author":[{"last_name":"Farjon","first_name":"Jonathan","full_name":"Farjon, Jonathan"},{"full_name":"Boisbouvier, Jérôme","first_name":"Jérôme","last_name":"Boisbouvier"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"},{"full_name":"Pardi, Arthur","last_name":"Pardi","first_name":"Arthur"},{"first_name":"Jean-Pierre","last_name":"Simorre","full_name":"Simorre, Jean-Pierre"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"}],"issue":"24","_id":"8476","publication":"Journal of the American Chemical Society","title":"Longitudinal-relaxation-enhanced NMR experiments for the study of nucleic acids in solution","month":"06","intvolume":"       131","oa_version":"None","publication_status":"published","date_created":"2020-09-18T10:11:49Z","article_processing_charge":"No","language":[{"iso":"eng"}],"page":"8571-8577","quality_controlled":"1","article_type":"original","publisher":"American Chemical Society"},{"publication_identifier":{"issn":["0002-7863","1520-5126"]},"day":"25","doi":"10.1021/ja809880p","abstract":[{"text":"An optimized NMR experiment that combines the advantages of methyl-TROSY and SOFAST-HMQC has been developed. It allows the recording of high quality methyl 1H−13C correlation spectra of protein assemblies of several hundreds of kDa in a few seconds. The SOFAST-methyl-TROSY-based experiment offers completely new opportunities for the study of structural and dynamic changes occurring in molecular nanomachines while they perform their biological function in vitro.","lang":"eng"}],"year":"2009","citation":{"mla":"Amero, Carlos, et al. “Fast Two-Dimensional NMR Spectroscopy of High Molecular Weight Protein Assemblies.” <i>Journal of the American Chemical Society</i>, vol. 131, no. 10, American Chemical Society, 2009, pp. 3448–49, doi:<a href=\"https://doi.org/10.1021/ja809880p\">10.1021/ja809880p</a>.","short":"C. Amero, P. Schanda, M.A. Durá, I. Ayala, D. Marion, B. Franzetti, B. Brutscher, J. Boisbouvier, Journal of the American Chemical Society 131 (2009) 3448–3449.","ista":"Amero C, Schanda P, Durá MA, Ayala I, Marion D, Franzetti B, Brutscher B, Boisbouvier J. 2009. Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. Journal of the American Chemical Society. 131(10), 3448–3449.","ama":"Amero C, Schanda P, Durá MA, et al. Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. <i>Journal of the American Chemical Society</i>. 2009;131(10):3448-3449. doi:<a href=\"https://doi.org/10.1021/ja809880p\">10.1021/ja809880p</a>","apa":"Amero, C., Schanda, P., Durá, M. A., Ayala, I., Marion, D., Franzetti, B., … Boisbouvier, J. (2009). Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja809880p\">https://doi.org/10.1021/ja809880p</a>","ieee":"C. Amero <i>et al.</i>, “Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies,” <i>Journal of the American Chemical Society</i>, vol. 131, no. 10. American Chemical Society, pp. 3448–3449, 2009.","chicago":"Amero, Carlos, Paul Schanda, M. Asunción Durá, Isabel Ayala, Dominique Marion, Bruno Franzetti, Bernhard Brutscher, and Jérôme Boisbouvier. “Fast Two-Dimensional NMR Spectroscopy of High Molecular Weight Protein Assemblies.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2009. <a href=\"https://doi.org/10.1021/ja809880p\">https://doi.org/10.1021/ja809880p</a>."},"date_updated":"2021-01-12T08:19:32Z","type":"journal_article","date_published":"2009-02-25T00:00:00Z","volume":131,"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","article_processing_charge":"No","date_created":"2020-09-18T10:12:01Z","oa_version":"None","publication_status":"published","intvolume":"       131","month":"02","title":"Fast two-dimensional NMR spectroscopy of high molecular weight protein assemblies","_id":"8477","publication":"Journal of the American Chemical Society","issue":"10","author":[{"full_name":"Amero, Carlos","last_name":"Amero","first_name":"Carlos"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"},{"full_name":"Durá, M. Asunción","last_name":"Durá","first_name":"M. Asunción"},{"full_name":"Ayala, Isabel","first_name":"Isabel","last_name":"Ayala"},{"last_name":"Marion","first_name":"Dominique","full_name":"Marion, Dominique"},{"last_name":"Franzetti","first_name":"Bruno","full_name":"Franzetti, Bruno"},{"first_name":"Bernhard","last_name":"Brutscher","full_name":"Brutscher, Bernhard"},{"full_name":"Boisbouvier, Jérôme","first_name":"Jérôme","last_name":"Boisbouvier"}],"publisher":"American Chemical Society","article_type":"original","quality_controlled":"1","page":"3448-3449","language":[{"iso":"eng"}]},{"type":"journal_article","date_published":"2009-02-09T00:00:00Z","year":"2009","citation":{"short":"S. Brüschweiler, P. Schanda, K. Kloiber, B. Brutscher, G. Kontaxis, R. Konrat, M. Tollinger, Journal of the American Chemical Society 131 (2009) 3063–3068.","mla":"Brüschweiler, Sven, et al. “Direct Observation of the Dynamic Process Underlying Allosteric Signal Transmission.” <i>Journal of the American Chemical Society</i>, vol. 131, no. 8, American Chemical Society, 2009, pp. 3063–68, doi:<a href=\"https://doi.org/10.1021/ja809947w\">10.1021/ja809947w</a>.","ista":"Brüschweiler S, Schanda P, Kloiber K, Brutscher B, Kontaxis G, Konrat R, Tollinger M. 2009. Direct observation of the dynamic process underlying allosteric signal transmission. Journal of the American Chemical Society. 131(8), 3063–3068.","ama":"Brüschweiler S, Schanda P, Kloiber K, et al. Direct observation of the dynamic process underlying allosteric signal transmission. <i>Journal of the American Chemical Society</i>. 2009;131(8):3063-3068. doi:<a href=\"https://doi.org/10.1021/ja809947w\">10.1021/ja809947w</a>","apa":"Brüschweiler, S., Schanda, P., Kloiber, K., Brutscher, B., Kontaxis, G., Konrat, R., &#38; Tollinger, M. (2009). Direct observation of the dynamic process underlying allosteric signal transmission. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja809947w\">https://doi.org/10.1021/ja809947w</a>","ieee":"S. Brüschweiler <i>et al.</i>, “Direct observation of the dynamic process underlying allosteric signal transmission,” <i>Journal of the American Chemical Society</i>, vol. 131, no. 8. American Chemical Society, pp. 3063–3068, 2009.","chicago":"Brüschweiler, Sven, Paul Schanda, Karin Kloiber, Bernhard Brutscher, Georg Kontaxis, Robert Konrat, and Martin Tollinger. “Direct Observation of the Dynamic Process Underlying Allosteric Signal Transmission.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2009. <a href=\"https://doi.org/10.1021/ja809947w\">https://doi.org/10.1021/ja809947w</a>."},"date_updated":"2021-01-12T08:19:33Z","abstract":[{"lang":"eng","text":"Allosteric regulation is an effective mechanism of control in biological processes. In allosteric proteins a signal originating at one site in the molecule is communicated through the protein structure to trigger a specific response at a remote site. Using NMR relaxation dispersion techniques we directly observe the dynamic process through which the KIX domain of CREB binding protein communicates allosteric information between binding sites. KIX mediates cooperativity between pairs of transcription factors through binding to two distinct interaction surfaces in an allosteric manner. We show that binding the activation domain of the mixed lineage leukemia (MLL) transcription factor to KIX induces a redistribution of the relative populations of KIX conformations toward a high-energy state in which the allosterically activated second binding site is already preformed, consistent with the Monod−Wyman−Changeux (WMC) model of allostery. The structural rearrangement process that links the two conformers and by which allosteric information is communicated occurs with a time constant of 3 ms at 27 °C. Our dynamic NMR data reveal that an evolutionarily conserved network of hydrophobic amino acids constitutes the pathway through which information is transmitted."}],"publication_identifier":{"issn":["0002-7863","1520-5126"]},"day":"09","doi":"10.1021/ja809947w","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","extern":"1","volume":131,"issue":"8","author":[{"full_name":"Brüschweiler, Sven","last_name":"Brüschweiler","first_name":"Sven"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul"},{"first_name":"Karin","last_name":"Kloiber","full_name":"Kloiber, Karin"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"},{"full_name":"Kontaxis, Georg","last_name":"Kontaxis","first_name":"Georg"},{"first_name":"Robert","last_name":"Konrat","full_name":"Konrat, Robert"},{"full_name":"Tollinger, Martin","first_name":"Martin","last_name":"Tollinger"}],"publication":"Journal of the American Chemical Society","_id":"8478","intvolume":"       131","title":"Direct observation of the dynamic process underlying allosteric signal transmission","month":"02","date_created":"2020-09-18T10:12:14Z","article_processing_charge":"No","publication_status":"published","oa_version":"None","language":[{"iso":"eng"}],"quality_controlled":"1","page":"3063-3068","article_type":"original","publisher":"American Chemical Society"},{"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"language":[{"iso":"eng"}],"oa_version":"None","month":"04","publication":"Journal of the American Chemical Society","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"type":"journal_article","date_published":"2009-04-01T00:00:00Z","publisher":"American Chemical Society","article_type":"original","quality_controlled":"1","page":"4233-4235","article_processing_charge":"No","date_created":"2023-08-01T10:30:17Z","publication_status":"published","intvolume":"       131","title":"Metal nanoparticles functionalized with molecular and supramolecular switches","scopus_import":"1","pmid":1,"_id":"13420","issue":"12","author":[{"last_name":"Klajn","first_name":"Rafal","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"},{"first_name":"Lei","last_name":"Fang","full_name":"Fang, Lei"},{"first_name":"Ali","last_name":"Coskun","full_name":"Coskun, Ali"},{"full_name":"Olson, Mark A.","last_name":"Olson","first_name":"Mark A."},{"full_name":"Wesson, Paul J.","first_name":"Paul J.","last_name":"Wesson"},{"full_name":"Stoddart, J. Fraser","first_name":"J. Fraser","last_name":"Stoddart"},{"full_name":"Grzybowski, Bartosz A.","first_name":"Bartosz A.","last_name":"Grzybowski"}],"volume":131,"extern":"1","day":"01","doi":"10.1021/ja9001585","abstract":[{"text":"Weakly protected metal nanoparticles (MNPs) are used as precursors for the preparation of catenane- and pseudorotaxane-decorated NPs of various compositions (gold, palladium, platinum). When attached to the surface of MNPs, the molecular switches retain their switching abilities. The redox potentials of these switches depend on and can be regulated by the composition of the mixed self-assembled monolayers covering the MNPs.","lang":"eng"}],"year":"2009","citation":{"ista":"Klajn R, Fang L, Coskun A, Olson MA, Wesson PJ, Stoddart JF, Grzybowski BA. 2009. Metal nanoparticles functionalized with molecular and supramolecular switches. Journal of the American Chemical Society. 131(12), 4233–4235.","short":"R. Klajn, L. Fang, A. Coskun, M.A. Olson, P.J. Wesson, J.F. Stoddart, B.A. Grzybowski, Journal of the American Chemical Society 131 (2009) 4233–4235.","mla":"Klajn, Rafal, et al. “Metal Nanoparticles Functionalized with Molecular and Supramolecular Switches.” <i>Journal of the American Chemical Society</i>, vol. 131, no. 12, American Chemical Society, 2009, pp. 4233–35, doi:<a href=\"https://doi.org/10.1021/ja9001585\">10.1021/ja9001585</a>.","chicago":"Klajn, Rafal, Lei Fang, Ali Coskun, Mark A. Olson, Paul J. Wesson, J. Fraser Stoddart, and Bartosz A. Grzybowski. “Metal Nanoparticles Functionalized with Molecular and Supramolecular Switches.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2009. <a href=\"https://doi.org/10.1021/ja9001585\">https://doi.org/10.1021/ja9001585</a>.","ieee":"R. Klajn <i>et al.</i>, “Metal nanoparticles functionalized with molecular and supramolecular switches,” <i>Journal of the American Chemical Society</i>, vol. 131, no. 12. American Chemical Society, pp. 4233–4235, 2009.","ama":"Klajn R, Fang L, Coskun A, et al. Metal nanoparticles functionalized with molecular and supramolecular switches. <i>Journal of the American Chemical Society</i>. 2009;131(12):4233-4235. doi:<a href=\"https://doi.org/10.1021/ja9001585\">10.1021/ja9001585</a>","apa":"Klajn, R., Fang, L., Coskun, A., Olson, M. A., Wesson, P. J., Stoddart, J. F., &#38; Grzybowski, B. A. (2009). Metal nanoparticles functionalized with molecular and supramolecular switches. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja9001585\">https://doi.org/10.1021/ja9001585</a>"},"date_updated":"2023-08-08T09:06:00Z","external_id":{"pmid":["19265400"]}},{"volume":129,"extern":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","doi":"10.1021/ja068949u","publication_identifier":{"issn":["0002-7863","1520-5126"]},"day":"17","abstract":[{"lang":"eng","text":"A technique is described that allows reducing acquisition times of multidimensional NMR experiments by extensive spectral folding. The method is simple and has many interesting applications for NMR studies of molecular structure, dynamics, and kinetics."}],"date_updated":"2021-01-12T08:19:36Z","year":"2007","citation":{"mla":"Lescop, Ewen, et al. “Automated Spectral Compression for Fast Multidimensional NMR and Increased Time Resolution in Real-Time NMR Spectroscopy.” <i>Journal of the American Chemical Society</i>, vol. 129, no. 10, American Chemical Society, 2007, pp. 2756–57, doi:<a href=\"https://doi.org/10.1021/ja068949u\">10.1021/ja068949u</a>.","short":"E. Lescop, P. Schanda, R. Rasia, B. Brutscher, Journal of the American Chemical Society 129 (2007) 2756–2757.","ista":"Lescop E, Schanda P, Rasia R, Brutscher B. 2007. Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. Journal of the American Chemical Society. 129(10), 2756–2757.","ama":"Lescop E, Schanda P, Rasia R, Brutscher B. Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. <i>Journal of the American Chemical Society</i>. 2007;129(10):2756-2757. doi:<a href=\"https://doi.org/10.1021/ja068949u\">10.1021/ja068949u</a>","apa":"Lescop, E., Schanda, P., Rasia, R., &#38; Brutscher, B. (2007). Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja068949u\">https://doi.org/10.1021/ja068949u</a>","chicago":"Lescop, Ewen, Paul Schanda, Rodolfo Rasia, and Bernhard Brutscher. “Automated Spectral Compression for Fast Multidimensional NMR and Increased Time Resolution in Real-Time NMR Spectroscopy.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2007. <a href=\"https://doi.org/10.1021/ja068949u\">https://doi.org/10.1021/ja068949u</a>.","ieee":"E. Lescop, P. Schanda, R. Rasia, and B. Brutscher, “Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy,” <i>Journal of the American Chemical Society</i>, vol. 129, no. 10. American Chemical Society, pp. 2756–2757, 2007."},"date_published":"2007-02-17T00:00:00Z","type":"journal_article","publisher":"American Chemical Society","article_type":"original","page":"2756-2757","quality_controlled":"1","language":[{"iso":"eng"}],"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"publication_status":"published","oa_version":"None","date_created":"2020-09-18T10:13:21Z","article_processing_charge":"No","title":"Automated spectral compression for fast multidimensional NMR and increased time resolution in real-time NMR spectroscopy","month":"02","intvolume":"       129","_id":"8486","publication":"Journal of the American Chemical Society","author":[{"full_name":"Lescop, Ewen","last_name":"Lescop","first_name":"Ewen"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda","first_name":"Paul"},{"full_name":"Rasia, Rodolfo","last_name":"Rasia","first_name":"Rodolfo"},{"full_name":"Brutscher, Bernhard","last_name":"Brutscher","first_name":"Bernhard"}],"issue":"10"},{"status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","volume":129,"abstract":[{"lang":"eng","text":"Following unidirectional biophysical events such as the folding of proteins or the equilibration of binding interactions, requires experimental methods that yield information at both atomic-level resolution and at high repetition rates. Toward this end a number of different approaches enabling the rapid acquisition of 2D NMR spectra have been recently introduced, including spatially encoded “ultrafast” 2D NMR spectroscopy and SOFAST HMQC NMR. Whereas the former accelerates acquisitions by reducing the number of scans that are necessary for completing arbitrary 2D NMR experiments, the latter operates by reducing the delay between consecutive scans while preserving sensitivity. Given the complementarities between these two approaches it seems natural to combine them into a single tool, enabling the acquisition of full 2D protein NMR spectra at high repetition rates. We demonstrate here this capability with the introduction of “ultraSOFAST” HMQC NMR, a spatially encoded and relaxation-optimized approach that can provide 2D protein correlation spectra at ∼1 s repetition rates for samples in the ∼2 mM concentration range. The principles, relative advantages, and current limitations of this new approach are discussed, and its application is exemplified with a study of the fast hydrogen−deuterium exchange characterizing amide sites in Ubiquitin."}],"publication_identifier":{"issn":["0002-7863","1520-5126"]},"day":"10","doi":"10.1021/ja066915g","type":"journal_article","date_published":"2007-01-10T00:00:00Z","citation":{"apa":"Gal, M., Schanda, P., Brutscher, B., &#38; Frydman, L. (2007). UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja066915g\">https://doi.org/10.1021/ja066915g</a>","ama":"Gal M, Schanda P, Brutscher B, Frydman L. UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. <i>Journal of the American Chemical Society</i>. 2007;129(5):1372-1377. doi:<a href=\"https://doi.org/10.1021/ja066915g\">10.1021/ja066915g</a>","ieee":"M. Gal, P. Schanda, B. Brutscher, and L. Frydman, “UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates,” <i>Journal of the American Chemical Society</i>, vol. 129, no. 5. American Chemical Society, pp. 1372–1377, 2007.","chicago":"Gal, Maayan, Paul Schanda, Bernhard Brutscher, and Lucio Frydman. “UltraSOFAST HMQC NMR and the Repetitive Acquisition of 2D Protein Spectra at Hz Rates.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2007. <a href=\"https://doi.org/10.1021/ja066915g\">https://doi.org/10.1021/ja066915g</a>.","mla":"Gal, Maayan, et al. “UltraSOFAST HMQC NMR and the Repetitive Acquisition of 2D Protein Spectra at Hz Rates.” <i>Journal of the American Chemical Society</i>, vol. 129, no. 5, American Chemical Society, 2007, pp. 1372–77, doi:<a href=\"https://doi.org/10.1021/ja066915g\">10.1021/ja066915g</a>.","short":"M. Gal, P. Schanda, B. Brutscher, L. Frydman, Journal of the American Chemical Society 129 (2007) 1372–1377.","ista":"Gal M, Schanda P, Brutscher B, Frydman L. 2007. UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates. Journal of the American Chemical Society. 129(5), 1372–1377."},"year":"2007","date_updated":"2021-01-12T08:19:37Z","article_type":"original","publisher":"American Chemical Society","keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"language":[{"iso":"eng"}],"quality_controlled":"1","page":"1372-1377","intvolume":"       129","title":"UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates","month":"01","date_created":"2020-09-18T10:13:27Z","article_processing_charge":"No","publication_status":"published","oa_version":"None","issue":"5","author":[{"full_name":"Gal, Maayan","first_name":"Maayan","last_name":"Gal"},{"last_name":"Schanda","first_name":"Paul","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"first_name":"Bernhard","last_name":"Brutscher","full_name":"Brutscher, Bernhard"},{"full_name":"Frydman, Lucio","last_name":"Frydman","first_name":"Lucio"}],"_id":"8487","publication":"Journal of the American Chemical Society"},{"type":"journal_article","date_published":"2006-06-21T00:00:00Z","year":"2006","citation":{"ista":"Schanda P, Van Melckebeke H, Brutscher B. 2006. Speeding up three-dimensional protein NMR experiments to a few minutes. Journal of the American Chemical Society. 128(28), 9042–9043.","short":"P. Schanda, H. Van Melckebeke, B. Brutscher, Journal of the American Chemical Society 128 (2006) 9042–9043.","mla":"Schanda, Paul, et al. “Speeding up Three-Dimensional Protein NMR Experiments to a Few Minutes.” <i>Journal of the American Chemical Society</i>, vol. 128, no. 28, American Chemical Society, 2006, pp. 9042–43, doi:<a href=\"https://doi.org/10.1021/ja062025p\">10.1021/ja062025p</a>.","chicago":"Schanda, Paul, Hélène Van Melckebeke, and Bernhard Brutscher. “Speeding up Three-Dimensional Protein NMR Experiments to a Few Minutes.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2006. <a href=\"https://doi.org/10.1021/ja062025p\">https://doi.org/10.1021/ja062025p</a>.","ieee":"P. Schanda, H. Van Melckebeke, and B. Brutscher, “Speeding up three-dimensional protein NMR experiments to a few minutes,” <i>Journal of the American Chemical Society</i>, vol. 128, no. 28. American Chemical Society, pp. 9042–9043, 2006.","apa":"Schanda, P., Van Melckebeke, H., &#38; Brutscher, B. (2006). Speeding up three-dimensional protein NMR experiments to a few minutes. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja062025p\">https://doi.org/10.1021/ja062025p</a>","ama":"Schanda P, Van Melckebeke H, Brutscher B. Speeding up three-dimensional protein NMR experiments to a few minutes. <i>Journal of the American Chemical Society</i>. 2006;128(28):9042-9043. doi:<a href=\"https://doi.org/10.1021/ja062025p\">10.1021/ja062025p</a>"},"date_updated":"2021-01-12T08:19:37Z","abstract":[{"text":"We demonstrate for different protein samples that three-dimensional HNCO and HNCA correlation spectra may be recorded in a few minutes acquisition time using the band-selective excitation short-transient sequences presented here. This opens new perspectives for the NMR structural investigation of unstable protein samples and real-time site-resolved studies of protein kinetics.","lang":"eng"}],"day":"21","publication_identifier":{"issn":["0002-7863","1520-5126"]},"doi":"10.1021/ja062025p","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","extern":"1","volume":128,"issue":"28","author":[{"first_name":"Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"first_name":"Hélène","last_name":"Van Melckebeke","full_name":"Van Melckebeke, Hélène"},{"last_name":"Brutscher","first_name":"Bernhard","full_name":"Brutscher, Bernhard"}],"_id":"8488","publication":"Journal of the American Chemical Society","intvolume":"       128","month":"06","title":"Speeding up three-dimensional protein NMR experiments to a few minutes","article_processing_charge":"No","date_created":"2020-09-18T10:13:36Z","oa_version":"None","publication_status":"published","keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"language":[{"iso":"eng"}],"quality_controlled":"1","page":"9042-9043","article_type":"original","publisher":"American Chemical Society"},{"author":[{"full_name":"Kalsin, Alexander M.","last_name":"Kalsin","first_name":"Alexander M."},{"last_name":"Kowalczyk","first_name":"Bartlomiej","full_name":"Kowalczyk, Bartlomiej"},{"full_name":"Smoukov, Stoyan K.","first_name":"Stoyan K.","last_name":"Smoukov"},{"last_name":"Klajn","first_name":"Rafal","full_name":"Klajn, Rafal","id":"8e84690e-1e48-11ed-a02b-a1e6fb8bb53b"},{"first_name":"Bartosz A.","last_name":"Grzybowski","full_name":"Grzybowski, Bartosz A."}],"issue":"47","_id":"13428","pmid":1,"scopus_import":"1","title":"Ionic-like behavior of oppositely charged nanoparticles","intvolume":"       128","publication_status":"published","article_processing_charge":"No","date_created":"2023-08-01T10:36:27Z","page":"15046-15047","quality_controlled":"1","article_type":"original","publisher":"American Chemical Society","external_id":{"pmid":["17117829"]},"date_updated":"2023-08-08T11:30:06Z","year":"2006","citation":{"short":"A.M. Kalsin, B. Kowalczyk, S.K. Smoukov, R. Klajn, B.A. Grzybowski, Journal of the American Chemical Society 128 (2006) 15046–15047.","mla":"Kalsin, Alexander M., et al. “Ionic-like Behavior of Oppositely Charged Nanoparticles.” <i>Journal of the American Chemical Society</i>, vol. 128, no. 47, American Chemical Society, 2006, pp. 15046–47, doi:<a href=\"https://doi.org/10.1021/ja0642966\">10.1021/ja0642966</a>.","ista":"Kalsin AM, Kowalczyk B, Smoukov SK, Klajn R, Grzybowski BA. 2006. Ionic-like behavior of oppositely charged nanoparticles. Journal of the American Chemical Society. 128(47), 15046–15047.","apa":"Kalsin, A. M., Kowalczyk, B., Smoukov, S. K., Klajn, R., &#38; Grzybowski, B. A. (2006). Ionic-like behavior of oppositely charged nanoparticles. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja0642966\">https://doi.org/10.1021/ja0642966</a>","ama":"Kalsin AM, Kowalczyk B, Smoukov SK, Klajn R, Grzybowski BA. Ionic-like behavior of oppositely charged nanoparticles. <i>Journal of the American Chemical Society</i>. 2006;128(47):15046-15047. doi:<a href=\"https://doi.org/10.1021/ja0642966\">10.1021/ja0642966</a>","chicago":"Kalsin, Alexander M., Bartlomiej Kowalczyk, Stoyan K. Smoukov, Rafal Klajn, and Bartosz A. Grzybowski. “Ionic-like Behavior of Oppositely Charged Nanoparticles.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2006. <a href=\"https://doi.org/10.1021/ja0642966\">https://doi.org/10.1021/ja0642966</a>.","ieee":"A. M. Kalsin, B. Kowalczyk, S. K. Smoukov, R. Klajn, and B. A. Grzybowski, “Ionic-like behavior of oppositely charged nanoparticles,” <i>Journal of the American Chemical Society</i>, vol. 128, no. 47. American Chemical Society, pp. 15046–15047, 2006."},"abstract":[{"lang":"eng","text":"Mixtures of oppositely charged nanoparticles of various sizes and charge ratios precipitate only at the point of electroneutrality. This phenomenonspecific to the nanoscale and reminiscent of threshold precipitation of ionsis a consequence of the formation of core-and-shell nanoparticle aggregates, in which the shells are composed of like-charged particles and are stabilized by efficient electrostatic screening."}],"doi":"10.1021/ja0642966","day":"29","extern":"1","volume":128,"publication":"Journal of the American Chemical Society","month":"11","oa_version":"None","language":[{"iso":"eng"}],"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"date_published":"2006-11-29T00:00:00Z","type":"journal_article","publication_identifier":{"issn":["0002-7863"],"eissn":["1520-5126"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public"},{"language":[{"iso":"eng"}],"keyword":["Colloid and Surface Chemistry","Biochemistry","General Chemistry","Catalysis"],"page":"8014-8015","quality_controlled":"1","article_type":"original","publisher":"American Chemical Society","author":[{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","last_name":"Schanda"},{"full_name":"Brutscher, Bernhard","first_name":"Bernhard","last_name":"Brutscher"}],"issue":"22","publication":"Journal of the American Chemical Society","_id":"8492","month":"05","title":"Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds","intvolume":"       127","oa_version":"None","publication_status":"published","date_created":"2020-09-18T10:14:05Z","article_processing_charge":"No","extern":"1","status":"public","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","volume":127,"date_published":"2005-05-14T00:00:00Z","type":"journal_article","date_updated":"2021-01-12T08:19:39Z","year":"2005","citation":{"ama":"Schanda P, Brutscher B. Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. <i>Journal of the American Chemical Society</i>. 2005;127(22):8014-8015. doi:<a href=\"https://doi.org/10.1021/ja051306e\">10.1021/ja051306e</a>","apa":"Schanda, P., &#38; Brutscher, B. (2005). Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. <i>Journal of the American Chemical Society</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/ja051306e\">https://doi.org/10.1021/ja051306e</a>","ieee":"P. Schanda and B. Brutscher, “Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds,” <i>Journal of the American Chemical Society</i>, vol. 127, no. 22. American Chemical Society, pp. 8014–8015, 2005.","chicago":"Schanda, Paul, and Bernhard Brutscher. “Very Fast Two-Dimensional NMR Spectroscopy for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of Seconds.” <i>Journal of the American Chemical Society</i>. American Chemical Society, 2005. <a href=\"https://doi.org/10.1021/ja051306e\">https://doi.org/10.1021/ja051306e</a>.","short":"P. Schanda, B. Brutscher, Journal of the American Chemical Society 127 (2005) 8014–8015.","mla":"Schanda, Paul, and Bernhard Brutscher. “Very Fast Two-Dimensional NMR Spectroscopy for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of Seconds.” <i>Journal of the American Chemical Society</i>, vol. 127, no. 22, American Chemical Society, 2005, pp. 8014–15, doi:<a href=\"https://doi.org/10.1021/ja051306e\">10.1021/ja051306e</a>.","ista":"Schanda P, Brutscher B. 2005. Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. Journal of the American Chemical Society. 127(22), 8014–8015."},"abstract":[{"lang":"eng","text":"We demonstrate for different protein samples that 2D 1H−15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle short-transient heteronuclear multiple quantum coherence experiment. This has enabled us to measure fast hydrogen−deuterium exchange rate constants along the backbone of a small globular protein fragment by real-time 2D NMR."}],"doi":"10.1021/ja051306e","publication_identifier":{"issn":["0002-7863","1520-5126"]},"day":"14"}]