Article ID Journal Published Year Pages File Type
8319970 Current Opinion in Structural Biology 2015 10 Pages PDF
Abstract
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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Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
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