A 30-residue fragment of the carp granulin-1 protein folds into a stack of two beta-hairpins similar to that found in the native protein.

TitleA 30-residue fragment of the carp granulin-1 protein folds into a stack of two beta-hairpins similar to that found in the native protein.
Publication TypeJournal Article
Year of Publication1999
AuthorsVranken, W. F., Z. G. Chen, P. Xu, S. James, H. P. Bennett, and F. Ni
JournalJ Pept Res
Volume53
Issue5
Pagination590-7
Date Published1999 May
ISSN1397-002X
KeywordsAmino Acid Sequence, Animals, Carps, Intercellular Signaling Peptides and Proteins, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Protein Structure, Secondary, Proteins
Abstract

Upon air oxidation, a peptide corresponding to the 30-residue N-terminal subdomain of carp granulin-1 spontaneously formed the disulfide pairing observed in the native protein. Structural characterization using NMR showed the presence of a defined secondary structure within this peptide. The chemical shifts for most of the alphaCH protons of the peptide and the protein are very similar, and the observed NOE contacts of the peptide strongly resemble those in the protein. A structure calculation of the peptide using NOE distance constraints indicates that the peptide fragment adopts the same conformation as formed within the native protein. The 30-residue N-terminal peptide of carp granulin-1 is the first example of an independently folded stack of two beta-hairpins reinforced by two interhairpin disulfide bonds. Two key areas of the structure show a clustering of hydrophobic residues that may account for its exceptional conformational stability.

Alternate JournalJ. Pept. Res.
PubMed ID10424355
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