Formation and stability of β-hairpin structures in polypeptides
Formation and stability of β-hairpin structures in polypeptides
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DOI：
10.1016/s0959-440x(98)80017-1
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发表时间：
1998-02-01
影响因子：
6.8
通讯作者：
Serrano, L
中科院分区：
文献类型：
--
作者：
Blanco, F;Ramírez-Alvarado, M;Serrano, L
对具有β-发夹结构的多肽模型的实验工作为这种二级结构元件的形成和稳定性提供了新的见解。转向区和反平行链残基不仅影响发夹的整体稳定性，还决定了发夹形成的类型。这些结果与对蛋白质中的β-折叠结构的实验和统计分析的结果相当吻合。
Experimental work on peptide models with beta-hairpin structures has provided new insights into the formation and stability of this secondary structure element. Both the turn region and the antiparallel strand residues not only affect the overall stability of the hairpin, but also determine the type of hairpin formed. These results agree reasonably well with those from experimental and statistical analyses of beta-sheet structures in proteins.