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Conformational studies of the C‐terminal 16‐amino‐acid‐residue fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus
Author(s) -
Skwierawska Agnieszka,
Ołdziej Stanisław,
Liwo Adam,
Scheraga Harold A.
Publication year - 2009
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21080
Subject(s) - chemistry , peptide , residue (chemistry) , amino acid , crystallography , peptide sequence , nuclear magnetic resonance spectroscopy , binding domain , protein structure , stereochemistry , binding site , biochemistry , gene
The structure and stability of the 16‐amino‐acid‐residue fragment [IG(46–61)] corresponding to the C‐terminal β‐hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus was investigated by means of CD and NMR spectroscopy and by differential scanning calorimetry. The CD and 2D NMR experiments were carried out (i) in water at different temperatures and (ii) at one temperature (305 K), with only CD, at different TFE concentrations. Our results show that the IG(46–61) peptide possesses organized three‐dimensional structure at all investigated temperatures. The three‐dimensional structure of the IG(46–61) peptide resembles the general shape of a β‐hairpin that is also observed for this peptide in the experimental structure of the B3 domain in the whole G protein; the structure is stabilized by hydrophobic interactions between nonpolar side chains. Our study shows that the melting temperature of the IG(46–61) peptide is about 320 K which supports the hypothesis that the investigated peptide can serve as a folding initiation site of the B3 domain of the immunoglobulin binding protein G. © 2008 Wiley Periodicals, Inc. Biopolymers 91: 37–51, 2009. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com