Cohen Rachel D, Pielak Gary J
Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina, 27599.
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina, 27599.
Protein Sci. 2017 Sep;26(9):1698-1703. doi: 10.1002/pro.3206. Epub 2017 Jun 12.
Anfinsen's thermodynamic hypothesis states that the native three-dimensional fold of a protein represents the structure with the lowest Gibbs free energy. Changes in the free energy of denaturation can arise from changes to the folded state, the unfolded state, or both. It has been recently recognized that quinary interactions, transient contacts that take place only in cells, can modulate protein stability through interactions involving the folded state. Here we show that the cellular environment can also remodel the unfolded state ensemble.
安芬森热力学假说指出,蛋白质的天然三维折叠结构代表着具有最低吉布斯自由能的结构。变性自由能的变化可能源于折叠态、未折叠态或两者的变化。最近人们认识到,五元相互作用,即仅在细胞中发生的瞬时接触,可以通过涉及折叠态的相互作用来调节蛋白质稳定性。在这里,我们表明细胞环境也可以重塑未折叠态集合。