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

✍ Scribed by E. Schievano; S. Mammi; E. Peggion

• Publisher: Wiley (John Wiley & Sons)
• Year: 1999
• Tongue: English
• Weight: 325 KB
• Volume: 50
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/(sici)1097-0282(199907)50:1<1::aid-bip1>3.0.co;2-v

✦ Synopsis

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 ␤-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 ␤-sheet conformation between the first and the last ␤-strand in the protein sequence, as well as a helical loop at the N-terminus of the polypeptide chain.