title: NMR studies of protein folding and binding in cells and cell-like environments.
abstract: Proteins function in cells where the concentration of macromolecules can exceed 300g/L. The ways in which this crowded environment affects the physical properties of proteins remain poorly understood. We summarize recent NMR-based studies of protein folding and binding conducted in cells and in vitro under crowded conditions. Many of the observations can be understood in terms of interactions between proteins and the rest of the intracellular environment (i.e. quinary interactions). Nevertheless, NMR studies of folding and binding in cells and cell-like environments remain in their infancy. The frontier involves investigations of larger proteins and further efforts in higher eukaryotic cells.
authors.affiliation: Department of Chemistry, University of North Carolina-Chapel Hill, Chapel Hill, NC 27599-3290, USA.
authors.forename: Austin E
authors.initials: AE
authors.lastname: Smith
authors.affiliation: Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan 430071, PR China.
authors.forename: Zeting
authors.initials: Z
authors.lastname: Zhang
authors.affiliation: Department of Chemistry, University of North Carolina-Chapel Hill, Chapel Hill, NC 27599-3290, USA; Department of Biochemistry and Biophysics, University of North Carolina-Chapel Hill, Chapel Hill, NC 27599-3290, USA. Electronic address: gary_pielak@unc.edu.
authors.forename: Gary J
authors.initials: GJ
authors.lastname: Pielak
authors.affiliation: Key Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan 430071, PR China. Electronic address: conggangli@wipm.ac.cn.
authors.forename: Conggang
authors.initials: C
authors.lastname: Li
mesh_terms: D003593:Cytoplasm / Q000378:metabolism*; D046911:Macromolecular Substances / Q000378:metabolism*; D008954:Models, Biological; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011485:Protein Binding; D017510:Protein Folding; D055550:Protein Stability
chemical_list: D046911:Macromolecular Substances