作者: Irisbel Guzman , Martin Gruebele
DOI: 10.1021/JP501866V
关键词: Biochemistry 、 Energy landscape 、 Protein folding 、 Proteome 、 Folding (chemistry) 、 Biophysics 、 Function (biology) 、 Cell 、 Cooperativity 、 Chemistry 、 Relaxation (NMR)
摘要: Protein folding is a remarkably fast unimolecular reaction, spanning microseconds to hours at room temperature. Thus, free energy differences and activation barriers on the landscape of proteins are rather small. This opens up possibility living cells modulating their protein’s landscapes, providing another way control function proteomes after transcriptional control, translational post-translational modification. In this Feature Article, we discuss advances in physicochemical studies protein stability inside cells. We focus particular our using relaxation imaging (FREI). Although effect cell landscapes only few kT, strong cooperativity many binding processes allows small modulation entropy produce large population modulation. Lastly, some biomolecular that particularly likely be affected by in-cell modul...