Sequence‐specific 1H‐NMR assignment and determination of the secondary structure of bovine heart fatty‐acid‐binding protein
Open Access
- 1 December 1992
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 210 (3) , 901-910
- https://doi.org/10.1111/j.1432-1033.1992.tb17494.x
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 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.Keywords
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