SEQUENCE-SPECIFIC H-1-NMR ASSIGNMENT AND DETERMINATION OF THE SECONDARY STRUCTURE OF BOVINE HEART FATTY-ACID-BINDING PROTEIN

被引:24
作者
LUCKE, C
LASSEN, D
KREIENKAMP, HJ
SPENER, F
RUTERJANS, H
机构
[1] UNIV FRANKFURT,INST BIOPHYS CHEM,THEODOR STERN KAI 7 HAUS 75A,W-6000 FRANKFURT,GERMANY
[2] UNIV MUNSTER,INST BIOCHEM,W-4400 MUNSTER,GERMANY
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 210卷 / 03期
关键词
D O I
10.1111/j.1432-1033.1992.tb17494.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The nearly complete sequence-specific H-1 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 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.
引用
收藏
页码:901 / 910
页数:10
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