Abstract
The nearly complete sequence-specific 1H resonance assignment of the pI = 4.9 isoform of cytosolic 15-kDa fatty-acid-binding protein from bovine heart (H-FABPc) 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 beta-strands and two short alpha-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.
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