Open AccessSequence‐specific 1 H‐NMR assignment and determination of the secondary structure of bovine heart fatty‐acid‐binding protein
Author(s) -
LÜCKE Christian,
LASSEN Dirck,
KREIENKAMP HansJürgen,
SPENER Friedrich,
RÜTERJANS Heinz
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb17494.x
Subject(s) - protein secondary structure , chemistry , sequence (biology) , fatty acid , stereochemistry , biochemistry
The nearly complete sequence‐specific 1 H resonance assignment of the pI = 4.9 isoform of cytosolic 15‐kDa fatty‐acid‐binding protein from bovine heart (H‐FABP c ) by homonuclear two‐dimensional NMR spectroscopy is presented. Regular secondary structure elements were identified from NOE spectra and the sequence locations of slowly exchanging backbone amide protons. The molecular structure of the protein was found to consist mainly of ten antiparallel β‐strands and two short α‐helices. The data presented here for the first time for a hydrophobic molecule transporter of the fatty‐acid‐binding protein type is the basis for a complete tertiary structure determination currently in progress.