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 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.
Schievano
E
E
Department of Organic Chemistry, University of Padova, Italy.
Mammi
S
S
Peggion
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics; D002645:Chickens; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids / Q000378:metabolism; D008099:Liver / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018996:Myelin P2 Protein / Q000737:chemistry* / Q000235:genetics; D009363:Neoplasm Proteins; D017433:Protein Structure, Secondary; D012996:Solutions
D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D018996:Myelin P2 Protein; D009363:Neoplasm Proteins; D012996:Solutions