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Default Determination of the secondary structural elements of chicken liver fatty acid bindin

Determination of the secondary structural elements of chicken liver fatty acid binding protein by two-dimensional homonuclear NMR.

Related Articles Determination of the secondary structural elements of chicken liver fatty acid binding protein by two-dimensional homonuclear NMR.

Biopolymers. 1999 Jul;50(1):1-11

Authors: Schievano E, Mammi S, Peggion E

A conformational study in solution of the fatty acid binding protein from chicken liver is presented. The nearly complete sequence-specific 1H resonance assignment was achieved from homonuclear two-dimensional nmr experiments using a sample of native protein. The principal elements of secondary structure were identified: 10 antiparallel beta-strands and one helical segment followed by a turn comprising 5 residues. These elements correspond closely with those of the crystal structure of the related protein, and two new secondary structural features obtained from the nmr data are the beta-sheet conformation between the first and the last beta-strand in the protein sequence, as well as a helical loop at the N-terminus of the polypeptide chain.

PMID: 10341664 [PubMed - indexed for MEDLINE]



Source: PubMed
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