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Conformational studies of the α‐helical 28–43 fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus
Author(s) -
Skwierawska Agnieszka,
RodziewiczMotowidło Sylwia,
Ołdziej Stanisław,
Liwo Adam,
Scheraga Harold A.
Publication year - 2008
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.21056
Subject(s) - chemistry , peptide , crystallography , folding (dsp implementation) , residue (chemistry) , helix (gastropod) , preprint , protein folding , stereochemistry , biochemistry , physics , ecology , quantum mechanics , snail , electrical engineering , biology , engineering
To determine whether the α‐helix in the B3 immunoglobulin binding domain of protein G from group G Streptococcus has conformational stability as an isolated fragment, we carried out a CD and NMR study of the 16‐residue peptide in solution corresponding to this α‐helix. Based on two‐dimensional H‐NMR spectra recorded at three different temperatures (283, 305, and 313 K), it was found that this peptide is mostly unstructured in water at these temperatures. Weak signals corresponding to i,i +3 or i,i +4 interactions, which are characteristic of formation of turn‐like structures, were observed in the ROE spectra at all temperatures. The absence of a stable three‐dimensional structure of the investigated peptide supports an earlier study (Blanco and Serrano, Eur J Biochem 1995, 230, 634–649) of a possible mechanism for folding of other (B1 and B2) immunoglobulin binding domains of Protein G. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 1032–1044, 2008. 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