Left-handed polyproline II helix formation is (very) locally driven
Left-handed polyproline II helix formation is (very) locally driven
复制标题
DOI：
10.1002/(sici)1097-0134(19981101)33:2
复制
发表时间：
1998-11-01
期刊：
影响因子：
--
通讯作者：
Creamer, TP
中科院分区：
文献类型：
--
作者：
Creamer, TP
左旋脯氨酸II螺旋（PPII）被认为是蛋白质序列中富含脯氨酸区域的首选构象。这些区域被假定为蛋白质-蛋白质相互作用域。本文采用简单的蒙特卡罗计算机模拟研究了这种结构的形成，采用硬球势，发现在模拟中脯氨酸序列只采用PPII结构。非脯氨酸、非甘氨酸残基作为客人插入到脯氨酸宿主肽中，受到以下脯氨酸残基的构象限制，并倾向于成为PPII螺旋的一部分。通过将两个丙氨酸残基插入到脯氨酸中，发现PPII结构不会通过多个非脯氨酸残基进行传播。这一发现对富含脯氨酸的区域将优先采用这种结构的假设提出了质疑，因为许多这样的序列由少于50%的脯氨酸残基组成。(C) 1998 Wiley-Liss, Inc。
The left-handed polyproline II helix (PPII) is believed to be the preferred conformation for proline-rich regions of sequence in proteins. Such regions have been postulated to be protein-protein interaction domains. The formation of this structure is studied here using simple Monte Carlo computer simulations employing the hard sphere potential, It is found that polyproline sequences adopt only the PPII structure in the simulations. Non-proline, non-glycine residues inserted as guests into polyproline host peptides are conformationally restricted by the following proline residues and tend to be part of the PPII helix. It is found through insertion of two alanine residues into polyproline that the PPII structure is not propagated through more than one non-proline residue. This finding calls into question the hypothesis that proline-rich regions will preferentially adopt this structure since many such sequences are comprised of less than 50% proline residues. (C) 1998 Wiley-Liss, Inc.