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Determination of the secondary structural elements of chicken liver fatty acid binding protein by two‐dimensional homonuclear NMR
Author(s) -
Schievano E.,
Mammi S.,
Peggion E.
Publication year - 1999
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/(sici)1097-0282(199907)50:1<1::aid-bip1>3.0.co;2-v
Subject(s) - homonuclear molecule , chemistry , nuclear magnetic resonance spectroscopy , biochemistry , stereochemistry , organic chemistry , molecule
A conformational study in solution of the fatty acid binding protein from chicken liver is presented. The nearly complete sequence‐specific 1 H 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 β‐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 β‐sheet conformation between the first and the last β‐strand in the protein sequence, as well as a helical loop at the N‐terminus of the polypeptide chain. © 1999 John Wiley & Sons, Inc. Biopoly 50: 1–11, 1999