Jackson S E
Chemical Laboratory, University of Cambridge, UK.
Fold Des. 1998;3(4):R81-91. doi: 10.1016/S1359-0278(98)00033-9.
Many small, monomeric proteins fold with simple two-state kinetics and show wide variation in folding rates, from microseconds to seconds. Thus, stable intermediates are not a prerequisite for the fast, efficient folding of proteins and may in fact be kinetic traps and slow the folding process. Using recent studies, can we begin to search for trends which may lead to a better understanding of the protein folding process?
许多小的单体蛋白以简单的两态动力学进行折叠,折叠速率变化范围很大,从微秒到秒不等。因此,稳定的中间体并非蛋白质快速、高效折叠的先决条件,实际上它们可能是动力学陷阱,会减缓折叠过程。基于最近的研究,我们能否开始寻找一些趋势,从而更好地理解蛋白质折叠过程呢?