Conformation of thymosin beta(9) in water/fluoroalcohol solution determined by NMR spectroscopy

被引：0
作者：
Stoll, R
Voelter, W
Holak, TA
机构：
[1] UNIV TUBINGEN,INST PHYSIOL CHEM,PHYS ABT,D-72076 TUBINGEN,GERMANY
[2] MAX PLANCK INST BIOCHEM,D-82152 MARTINSRIED,GERMANY
来源：
BIOPOLYMERS | 1997年 / 41卷 / 06期
关键词：
beta-thymosins; actin-binding peptide; conformation; nmr;
D O I：
10.1002/(SICI)1097-0282(199705)41:6<623::AID-BIP3>3.0.CO;2-S
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 conformation of thymosin beta(9) in solution of 40% (v/v) 1,1,1,3, 3, 3-hexafluoro-2-propanol-d(2) in water has been investigated by two-dimensional H-1-nmr spectroscopy. Under this condition thymosin beta(9) adopts an ordered structure. The determination of the conformation of the peptide was based on a set of 304 approximate interproton distance constraints derived from nuclear Overhauser enhancement measurements. The conformation of thymosin beta(9) includes two helical regions from residues 4 to 27 and 32 to 41. The two helices are separated by a poorly defined loop region between amino acids 28 and 31; the N-terminus of thymosin beta(9) shows random-coil structure only. (C) 1997 John Wiley & Sons, Inc.
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收藏
页码：623 / 634
页数：12
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