Turn residue sequence determines β-hairpin conformation in designed peptides

Journal of the American Chemical Society

Volumn 119, Issue 1, 1997, Pages 175-183

  De Alba, Eva ^a   Jiménez, M Angeles ^a   Rico, Manuel ^a  

^a INSTITUTO DE ESTRUCTURA DE LA MATERIA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN FOLDING; PROTEIN STRUCTURE; THEORY;

EID: 1842403587     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja962325e     Document Type: Article

References (55)

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23. (a) The different types of β-hairpin conformations and turns connecting the two strands in each β-hairpin were named according to the classification proposed by: Sibanda, B. L.; Thornton, J. M. Methods Enzymol. 1991, 202, 59-82. Sibanda, B. L.; Blundell, T. L.; Thornton, J. M. J. Mol. Biol. 1989, 206, 759-777. The β-hairpin shown in Figure 2a is a β-hairpin 2:2 because it contains two residues at the loop region, and the distal strand residues, S17 and Y20, have two hydrogen bonds, while the β-hairpin shown in Figure 2b is a β-hairpin 3:5 because it has three residues at the loop region and the distal strand residues, N17 and S21, have only one hydrogen bond, and the β-hairpin shown in Figure 2c is a β-hairpin 4:4 since it contains four residues at the loop region and the distal strand residues, S3 and X8, have two hydrogen bonds.
24. (a) The different types of β-hairpin conformations and turns connecting the two strands in each β-hairpin were named according to the classification proposed by: Sibanda, B. L.; Thornton, J. M. Methods Enzymol. 1991, 202, 59-82. Sibanda, B. L.; Blundell, T. L.; Thornton, J. M. J. Mol. Biol. 1989, 206, 759-777. The β-hairpin shown in Figure 2a is a β-hairpin 2:2 because it contains two residues at the loop region, and the distal strand residues, S17 and Y20, have two hydrogen bonds, while the β-hairpin shown in Figure 2b is a β-hairpin 3:5 because it has three residues at the loop region and the distal strand residues, N17 and S21, have only one hydrogen bond, and the β-hairpin shown in Figure 2c is a β-hairpin 4:4 since it contains four residues at the loop region and the distal strand residues, S3 and X8, have two hydrogen bonds.
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54. Conformational properties of peptides with strand mutations is now in progress to better determine the importance of β-strand residues on the stability of β-hairpin structures.
55. 27 For example, in the β-hairpin 3:5 shown in Figure 2d, the pair Y2-T10 is in a hydrogen-bonded site and the pair S3-W9 in a non-hydrogen-bonded site.