Harrison S C, Durbin R
Proc Natl Acad Sci U S A. 1985 Jun;82(12):4028-30. doi: 10.1073/pnas.82.12.4028.
We argue that folding of the compact domains of proteins can occur with adequate rapidity in the absence of a unique directed mechanism, provided that native-like local structure dominates the folding process. We further suggest that the evolution of amino acid sequences should favor multiple paths to the folded state. Existing physicochemical and mutational data are not inconsistent with a many-pathway model. The analogy of a jigsaw puzzle, with multiple routes to a unique solution, appears to be particularly apt.
我们认为,倘若类天然的局部结构主导折叠过程,那么在没有独特定向机制的情况下,蛋白质紧密结构域的折叠也能够以足够快的速度发生。我们进一步提出,氨基酸序列的进化应有利于形成多种通向折叠态的途径。现有的物理化学和突变数据与多途径模型并不矛盾。拼图游戏有多种途径可得到唯一解,这一类比似乎特别恰当。