FOLDING OF POLYPEPTIDE CHAINS IN PROTEINS - PROPOSED MECHANISM FOR FOLDING
FOLDING OF POLYPEPTIDE CHAINS IN PROTEINS - PROPOSED MECHANISM FOR FOLDING
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DOI：
10.1073/pnas.68.9.2293
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发表时间：
1971-01-01
影响因子：
11.1
通讯作者：
SCHERAGA, HA
中科院分区：
文献类型：
--
作者：
LEWIS, PN;MOMANY, FA;SCHERAGA, HA
提出了一种蛋白质链折叠的机制。基于短程相互作用，某些氨基酸序列具有高度的倾向性，例如α-螺旋。然而，这些短螺旋（或其他有序）区域只能通过两个这样的有序区域的邻近产生的长程相互作用来稳定。这些区域通过某些其他氨基酸序列的直接影响彼此靠近，这些氨基酸序列也基于短程相互作用具有形成β-弯曲或其变体的高概率。对各种氨基酸发生β-弯曲的趋势进行分析，并且可以高度可靠地预测其中将发生β-弯曲的链的区域。
A mechanism is proposed for the folding of protein chains. On the basis of short-range interactions, certain aminoacid sequences have a high propensity to be, say, α-helical. However, these short helical (or other ordered) regions can be stabilized only by long-range interactions arising from the proximity of two such ordered regions. These regions are brought near each other by the directing influence of certain other aminoacid sequences that have a high probability of forming β-bends or variants thereof, also on the basis of short-range interactions. An analysis is made of the tendency of various amino acids to occur in β-bends, and it is possible to predict the regions of a chain in which a β-bend will occur with a high degree of reliability.