The supramolecular chemistry of β-sheets.
The supramolecular chemistry of β-sheets.
复制标题
DOI:
10.1021/ja3088407
复制
发表时间:
2013-04-17
影响因子:
15
通讯作者:
Nowick, James S.
中科院分区:
文献类型:
--
作者:
Cheng, Pin-Nan;Pham, Johnny D.;Nowick, James S.
Interactions among β-sheets occur widely in protein quaternary structure, protein-protein interaction, and protein aggregation and are central in Alzheimer’s and other amyloid-related diseases. This Perspective looks at the structural biology of these important yet under-appreciated interactions from a supramolecular chemist’s point of view. Common themes in the supramolecular interactions of β-sheets are identified and richly illustrated though examples from proteins, amyloids, and chemical model systems. β-Sheets interact through edge-to-edge hydrogen bonding to form extended layers and through face-to-face hydrophobic or van der Waals interactions to form layered sandwich-like structures. Side chains from adjacent layers can fit together through simple hydrophobic contacts or can participate in complementary interdigitation or knob-hole interactions. The layers can be aligned, offset, or rotated. The right-handed twist of β-sheets provides additional opportunities for stabilization of edge-to-edge contacts and rotated layered structures.
登录
查看更多内容
影响因子:
21.8
作者:
通讯作者:
--
影响因子:
3.6
作者:
Cheng, Pin-Nan;Nowick, James S.
通讯作者:
Nowick, James S.
影响因子:
5.8
作者:
Dou, YM;Baisnée, PF;Baldi, P
通讯作者:
Baldi, P
DOI:
10.1073/pnas.0910080106
发表时间:
2009-11-10
影响因子:
11.1
作者:
Ivanova, Magdalena I.;Sievers, Stuart A.;Eisenberg, David
通讯作者:
Eisenberg, David
DOI:
10.1107/s0907444996003307
发表时间:
1996-09-01
期刊:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子:
--
作者:
Damas, AM;Ribeiro, S;Saraiva, MJ
通讯作者:
Saraiva, MJ