@article{14036,
  abstract     = {Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is establishing itself as a powerful method for the characterization of protein dynamics at the atomic scale. We discuss here how R1ρ MAS relaxation dispersion NMR can explore microsecond-to-millisecond motions. Progress in instrumentation, isotope labeling, and pulse sequence design has paved the way for quantitative analyses of even rare structural fluctuations. In addition to isotropic chemical-shift fluctuations exploited in solution-state NMR relaxation dispersion experiments, MAS NMR has a wider arsenal of observables, allowing to see motions even if the exchanging states do not differ in their chemical shifts. We demonstrate the potential of the technique for probing motions in challenging large enzymes, membrane proteins, and protein assemblies.},
  author       = {Napoli, Federico and Becker, Lea Marie and Schanda, Paul},
  issn         = {1879-033X},
  journal      = {Current Opinion in Structural Biology},
  number       = {10},
  publisher    = {Elsevier},
  title        = {{Protein dynamics detected by magic-angle spinning relaxation dispersion NMR}},
  doi          = {10.1016/j.sbi.2023.102660},
  volume       = {82},
  year         = {2023},
}

@article{11167,
  abstract     = {Complex I is one of the major respiratory complexes, conserved from bacteria to mammals. It oxidises NADH, reduces quinone and pumps protons across the membrane, thus playing a central role in the oxidative energy metabolism. In this review we discuss our current state of understanding the structure of complex I from various species of mammals, plants, fungi, and bacteria, as well as of several complex I-related proteins. By comparing the structural evidence from these systems in different redox states and data from mutagenesis and molecular simulations, we formulate the mechanisms of electron transfer and proton pumping and explain how they are conformationally and electrostatically coupled. Finally, we discuss the structural basis of the deactivation phenomenon in mammalian complex I.},
  author       = {Kampjut, Domen and Sazanov, Leonid A},
  issn         = {0959-440X},
  journal      = {Current Opinion in Structural Biology},
  keywords     = {Molecular Biology, Structural Biology},
  publisher    = {Elsevier},
  title        = {{Structure of respiratory complex I – An emerging blueprint for the mechanism}},
  doi          = {10.1016/j.sbi.2022.102350},
  volume       = {74},
  year         = {2022},
}

@article{6343,
  abstract     = {Cryo-electron tomography (cryo-ET) provides unprecedented insights into the molecular constituents of biological environments. In combination with an image processing method called subtomogram averaging (STA), detailed 3D structures of biological molecules can be obtained in large, irregular macromolecular assemblies or in situ, without the need for purification. The contextual meta-information these methods also provide, such as a protein’s location within its native environment, can then be combined with functional data. This allows the derivation of a detailed view on the physiological or pathological roles of proteins from the molecular to cellular level. Despite their tremendous potential in in situ structural biology, cryo-ET and STA have been restricted by methodological limitations, such as the low obtainable resolution. Exciting progress now allows one to reach unprecedented resolutions in situ, ranging in optimal cases beyond the nanometer barrier. Here, I review current frontiers and future challenges in routinely determining high-resolution structures in in situ environments using cryo-ET and STA.},
  author       = {Schur, Florian KM},
  issn         = {0959-440X},
  journal      = {Current Opinion in Structural Biology},
  number       = {10},
  pages        = {1--9},
  publisher    = {Elsevier},
  title        = {{Toward high-resolution in situ structural biology with cryo-electron tomography and subtomogram averaging}},
  doi          = {10.1016/j.sbi.2019.03.018},
  volume       = {58},
  year         = {2019},
}

@article{10355,
  abstract     = {The molecular machinery of life is largely created via self-organisation of individual molecules into functional assemblies. Minimal coarse-grained models, in which a whole macromolecule is represented by a small number of particles, can be of great value in identifying the main driving forces behind self-organisation in cell biology. Such models can incorporate data from both molecular and continuum scales, and their results can be directly compared to experiments. Here we review the state of the art of models for studying the formation and biological function of macromolecular assemblies in living organisms. We outline the key ingredients of each model and their main findings. We illustrate the contribution of this class of simulations to identifying the physical mechanisms behind life and diseases, and discuss their future developments.},
  author       = {Hafner, Anne E and Krausser, Johannes and Šarić, Anđela},
  issn         = {0959-440X},
  journal      = {Current Opinion in Structural Biology},
  keywords     = {molecular biology, structural biology},
  pages        = {43--52},
  publisher    = {Elsevier},
  title        = {{Minimal coarse-grained models for molecular self-organisation in biology}},
  doi          = {10.1016/j.sbi.2019.05.018},
  volume       = {58},
  year         = {2019},
}