Formation and stability of β-hairpin structures in polypeptides

Current Opinion in Structural Biology

Volumn 8, Issue 1, 1998, Pages 107-111

  Blanco, Francisco ^a   Ramírez Alvarado, Marina ^a   Serrano, Luis ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE;

KINETICS; MOLECULAR DYNAMICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SHORT SURVEY;

EID: 0032006708     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80017-1     Document Type: Article

References (29)

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15. of outstanding interest Ramirez-Alvarado M, Blanco FJ, Serrano L. De novo design and structural analysis of a model β-hairpin peptide system. Nat Struct Biol. 3:1996;604-612 This paper describes a peptide designed completely de novo that folds as a monomeric β sheet. Substitution of the strand residues by alanine results in abolishment of the hairpin structure, suggesting that sidechain - sidechain interactions contribute significantly to hairpin stability.
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17. of outstanding interest Haque TS, Gellman SH. Insights on β-hairpin stability in aqueous solution from peptides with enforced type I′ and type II′ β-turns. J Am Chem Soc. 1197:1997;2303-2304 The authors have done an interesting study incorporating D-stereoisomers residues at one or both turn positions of a 16-residue peptide that corresponds to the N-terminal segment of ubiquitin, in order to create "mirror image turns". Their results indicate that type I′ and type II′ β turns are required for the formation of a two-residue turn β hairpin.
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19. of outstanding interest Ramírez-Alvarado M, Blanco FJ, Niemann H, Serrano L. Role of β-turn residues in β-hairpin formation and stability in designed peptides. J Mol Biol. 273:1997;898-912 Mutagenesis of the first central residue in the type I′ β turn from a model peptide system that folds as a β hairpin shows the importance of the turn in hairpin stability and illustrates the idea that the presence of the turn does necessarily alter the pairing of the strands. Interestingly, there is a very good correlation between the effect of the different residues on hairpin stability and their relative abundance in the protein database.
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