Left‐handed topology of super‐secondary structure formed by aligned α‐helix and β‐hairpin

FEBS Letters

Kajava, A.V.¹ 

[1] Institute of Protein Research, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia

关键词: α-Helix;    β-Hairpin;    Super-secondary structure;    Amino acid sequence;    Prediction;   

DOI  :  10.1016/0014-5793(92)80271-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel super-secondary structure common for many non-homological proteins is considered. This folding pattern, consisting of adjacent along the chain α-helix and β-hairpin, has an aligned packing. It is found that one of the two possible ‘mirror-symmetrical’ topologies is observed in proteins. The α-helix + β-hairpin structures have a similar pattern of hydrophobic residues in their amino acid sequences. The remaining part of a molecule or a domain is almost always located on the same side of the considered folding pattern. These results can be used in the prediction of three-dimensional protein structure and protein design.

【 授权许可】

Unknown