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

A conformational study in solution of the fatty acid binding protein from c hicken liver is presented. The nearly complete sequence-specific H-1 resona nce assignment was achieved from homonuclear two-dimensional nmr experiment s using a sample of native protein. The principal elements of secondary str ucture were identified: 10 antiparallel beta-strands and one helical segmen t followed by a turn comprising 5 residues. These elements correspond close ly 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 seq uence, as well as a helical loop at the N-terminus of the polypeptide chain . (C) 1999 John Wiley & Sons, Inc.