Abstract：
:Autonomously folding beta-hairpins have recently emerged as powerful tools for elucidating the origins of antiparallel beta-sheet folding preferences. Analysis of such model systems has suggested four potential sources of beta-sheet stability: (1) the conformational propensity of the loop segment that connects adjacent strands; (2) favorable contacts between side-chains on adjacent strands; (3) interstrand hydrogen bonds; and (4) the intrinsic beta-sheet propensities of the strand residues. We describe the design and analysis of a series of isomeric 20 residue peptides in which factors (1)-(4) are identical. Differences in beta-hairpin formation within this series demonstrate that these four factors, individually, are not sufficient to explain beta-sheet stability. In agreement with the prediction of a simple statistical mechanical model for beta-hairpin formation, our results show that the separation between the loop segment and an interstrand cluster of hydrophobic side-chains strongly influences beta-hairpin size and stability, with a smaller separation leading to greater stability.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Espinosa JF,Muñoz V,Gellman SHdoi
10.1006/jmbi.2000.4349keywords:
subject
Has Abstractpub_date
2001-02-23 00:00:00pages
397-402issue
3eissn
0022-2836issn
1089-8638pii
S0022-2836(00)94349-3journal_volume
306pub_type
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