CROSS-HELIX SEPARATION OF TROPOMYOSIN MOLECULES IN ACTO-TROPOMYOSIN AS DETERMINED BY NEUTRON-SCATTERING

被引：18

作者：

BIVIN, DB

STONE, DB

SCHNEIDER, DK

MENDELSON, RA

机构：

[1] UNIV CALIF SAN FRANCISCO,CARDIOVASC RES INST,SAN FRANCISCO,CA 94143

[2] UNIV CALIF SAN FRANCISCO,DEPT BIOCHEM & BIOPHYS,SAN FRANCISCO,CA 94143

[3] BROOKHAVEN NATL LAB,DIV BIOL,UPTON,NY 11973

来源：

BIOPHYSICAL JOURNAL | 1991年 / 59卷 / 04期

关键词：

D O I：

10.1016/S0006-3495(91)82300-1

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The cross-helix separation of Tm molecules in acto-tropomyosin has been determined using neutron scattering. Deuterated Dictyostelium discoideum actin was density matched in a 93% D2O buffer so that effectively only the protonated tropomyosin was "visible" to neutrons. Analysis of the solution scattering pattern in the region of the first oscillation yielded a value for the cross-helix separation of 7.9 +/- 0.3 nm. The implications of this value for the mechanism of the regulation of muscle contraction are discussed in light of recent results by others.

引用

页码：880 / 888

页数：9

共 33 条

[21] STRUCTURAL ROLE OF TROPOMYOSIN IN MUSCLE REGULATION - ANALYSIS OF X-RAY-DIFFRACTION PATTERNS FROM RELAXED AND CONTRACTING MUSCLES [J].