Martin J, Hartl F U
Cellular Biochemisty and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA.
Structure. 1993 Nov 15;1(3):161-4. doi: 10.1016/0969-2126(93)90017-b.
In vitro, many unfolded polypeptides are able to fold to the native state spontaneously, indicating that the amino acid sequence of a protein contains all the information necessary to specify its three-dimensional conformation. It had been assumed that protein folding in vivo also generally occurs in a spontaneous process. This view has changed only recently due to the discovery of a number of proteins, now commonly called 'molecular chaperones', which are essential for cellular protein folding and occur ubiquitously in eubacteria, archaebacteria and in eukaryotic cells.
在体外，许多未折叠的多肽能够自发折叠成天然状态，这表明蛋白质的氨基酸序列包含了指定其三维构象所需的所有信息。人们曾认为体内蛋白质折叠通常也是一个自发过程。直到最近，由于发现了一些现在通常被称为“分子伴侣”的蛋白质，这种观点才发生了改变。这些分子伴侣对于细胞内蛋白质折叠至关重要，普遍存在于真细菌、古细菌和真核细胞中。
