CRYSTAL-STRUCTURE AND MOLECULAR-INTERACTIONS OF TROPOMYOSIN

被引：121

作者：

PHILLIPS, GN

LATTMAN, EE

CUMMINS, P

LEE, KY

COHEN, C

机构：

[1] Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham

[2] Department of Biophysics, Johns Hopkins University, School of Medicine, Baltimore

[3] Department of Cardiovascular Medicine, University of Birmingham, Queen Elizabeth Hospital, Birmingham

来源：

NATURE | 1979年 / 278卷 / 5703期

关键词：

D O I：

10.1038/278413a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The three-dimensional structure of tropomyosin filaments has been determined by x-ray crystallography. The ends of the molecules were located by reference to the single pair of cysteine residues. Departures from the α-helical-coiled coil conformation may occur in localised domains along the molecule as well as at the overlapping ends. © 1979 Nature Publishing Group.

引用

页码：413 / 417

页数：5

共 33 条

[1] TROPOMYOSIN - A NEW ASYMMETRIC PROTEIN COMPONENT OF THE MUSCLE FIBRIL [J].