Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 30, Issue -, Pages 7-16Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2014.10.004
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Funding
- Ministry of Science and Technology of China [2013CB910200]
- 1000 Young Talents Program
- National Natural Science Foundation of China [21075134]
- U.S. National Science Foundation [MCB-1051819, MCB-1410854]
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Proteins function in cells where the concentration of macromolecules can exceed 300 g/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.
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