Structures of helical β-tapes and twisted ribbons:: The role of side-chain interactions on twist and bend behavior
Structures of helical β-tapes and twisted ribbons:: The role of side-chain interactions on twist and bend behavior
复制标题
DOI：
10.1021/nl034095p
复制
发表时间：
2003-11-01
期刊：
影响因子：
10.8
通讯作者：
Boden, N
中科院分区：
文献类型：
--
作者：
Fishwick, CWG;Beevers, AJ;Boden, N
分子动力学（MD）模拟已被用于获得对由自组装肽P-11-I（CH 3CO-OORQQQQQEQQ-NH 2）和P-11-II（CH 3CO-QQRFOWQFEQQ-NH 2）形成的带状和带状（双带）样P-折叠聚集体的扭曲、弯曲和螺旋节距的起源的分子洞察。P-11-II与P-11-I的不同之处在于，在位置4、6和8处的谷氨酰胺已被F、W和F取代，并且这产生了具有显著更短螺旋节距的左旋螺旋带。这些疏水残基的存在也增强了P-11-II条带中的交叉带吸引力，这缩短了螺旋螺距。
Molecular Dynamics (MD) simulations have been used to obtain a molecular insight into the origins of the twist, bend, and helix pitch of the tape-like and ribbon (double tape)-like P-sheet aggregates formed by the self-assembling peptides P-11-I (CH 3CO-OORQQQQQEQQ-NH2) and P-11-II (CH3CO-QQRFOWQFEQQ-NH2). P-11-II differs from P-11-I in that glutamines at positions 4, 6, and 8 have been substituted for F, W, and F, and this gives rise to left-handed helicoidal tapes having a significantly shorter helix pitch. The presence of these hydrophobic residues also enhances the cross-tape attractive forces in P-11-II ribbons, which foreshortens the helix pitch.