H-1-NMR SPECTROSCOPY REVEALS THAT MOUSE HSP25 HAS A FLEXIBLE C-TERMINAL EXTENSION OF 18 AMINO-ACIDS

被引：56
作者：
CARVER, JA
ESPOSITO, G
SCHWEDERSKY, G
GAESTEL, M
机构：
[1] UNIV UDINE,DIPARTIMENTO SCI & TECNOL BIOMED,I-33100 UDINE,ITALY
[2] MAX DELBRUCK CENTRUM MOLEK MED,BERLIN,GERMANY
来源：
FEBS LETTERS | 1995年 / 369卷 / 2-3期
关键词：
SMALL HEAT-SHOCK PROTEIN; CHAPERONE; ALPHA-CRYSTALLIN; NMR SPECTROSCOPY; FLEXIBILITY;
D O I：
10.1016/0014-5793(95)00770-A
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 small heat-shock proteins (Hsps) exist as large and stabilising non-native proteins in a chaperone-like manner. Two-dimensional H-1 NMR spectroscopy of mouse Hsp25 reveals that the last 18 amino acids have great flexibility with motion that is essentially independent of the domain care of the protein. The lens protein, alpha-crystallin, is homologous to Hsp25 and its two subunits also have flexible C-terminal extensions. The flexible region in Hsp25 encompasses exactly that expected from sequence comparison with alpha-crystallin implying that both proteins have similar structures and that the C-terminal extensions could be of functional importance for both proteins.
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页码：305 / 310
页数：6
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