@article{8487,
  abstract     = {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.},
  author       = {Gal, Maayan and Schanda, Paul and Brutscher, Bernhard and Frydman, Lucio},
  issn         = {0002-7863},
  journal      = {Journal of the American Chemical Society},
  keywords     = {Colloid and Surface Chemistry, Biochemistry, General Chemistry, Catalysis},
  number       = {5},
  pages        = {1372--1377},
  publisher    = {American Chemical Society},
  title        = {{UltraSOFAST HMQC NMR and the repetitive acquisition of 2D protein spectra at Hz rates}},
  doi          = {10.1021/ja066915g},
  volume       = {129},
  year         = {2007},
}

@article{13428,
  abstract     = {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.},
  author       = {Kalsin, Alexander M. and Kowalczyk, Bartlomiej and Smoukov, Stoyan K. and Klajn, Rafal and Grzybowski, Bartosz A.},
  issn         = {1520-5126},
  journal      = {Journal of the American Chemical Society},
  keywords     = {Colloid and Surface Chemistry, Biochemistry, General Chemistry, Catalysis},
  number       = {47},
  pages        = {15046--15047},
  publisher    = {American Chemical Society},
  title        = {{Ionic-like behavior of oppositely charged nanoparticles}},
  doi          = {10.1021/ja0642966},
  volume       = {128},
  year         = {2006},
}

@article{13429,
  abstract     = {The fruitful core: Organic syntheses reported in the literature from 1850 to 2004 are analyzed with mathematical tools from network theory and statistical physics. There is a set of substances (the core) from which the majority of other organic compounds can be made (see picture; red: core, blue: periphery, green: islands). Search algorithms are used to identify small optimal sets of maximally useful chemicals.},
  author       = {Bishop, Kyle J. M. and Klajn, Rafal and Grzybowski, Bartosz A.},
  issn         = {1521-3773},
  journal      = {Angewandte Chemie International Edition},
  keywords     = {General Chemistry, Catalysis},
  number       = {32},
  pages        = {5348--5354},
  publisher    = {Wiley},
  title        = {{The core and most useful molecules in organic chemistry}},
  doi          = {10.1002/anie.200600881},
  volume       = {45},
  year         = {2006},
}

@article{8488,
  abstract     = {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.},
  author       = {Schanda, Paul and Van Melckebeke, Hélène and Brutscher, Bernhard},
  issn         = {0002-7863},
  journal      = {Journal of the American Chemical Society},
  keywords     = {Colloid and Surface Chemistry, Biochemistry, General Chemistry, Catalysis},
  number       = {28},
  pages        = {9042--9043},
  publisher    = {American Chemical Society},
  title        = {{Speeding up three-dimensional protein NMR experiments to a few minutes}},
  doi          = {10.1021/ja062025p},
  volume       = {128},
  year         = {2006},
}

@article{8492,
  abstract     = {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.},
  author       = {Schanda, Paul and Brutscher, Bernhard},
  issn         = {0002-7863},
  journal      = {Journal of the American Chemical Society},
  keywords     = {Colloid and Surface Chemistry, Biochemistry, General Chemistry, Catalysis},
  number       = {22},
  pages        = {8014--8015},
  publisher    = {American Chemical Society},
  title        = {{Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds}},
  doi          = {10.1021/ja051306e},
  volume       = {127},
  year         = {2005},
}