肌球蛋白头部的结构域、运动及调节 - Suppr

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超能文献

Domains, motions and regulation in the myosin head.

作者信息

Vibert P, Cohen C

机构信息

Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.

出版信息

J Muscle Res Cell Motil. 1988 Aug;9(4):296-305. doi: 10.1007/BF01773873.

DOI:10.1007/BF01773873

PMID:3065358

Abstract

摘要

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Domains, motions and regulation in the myosin head.肌球蛋白头部的结构域、运动及调节

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本文引用的文献

Structural models for the regulatory switch of Myosin.肌球蛋白调节开关的结构模型。

Biophys J. 1986 Jan;49(1):131-3. doi: 10.1016/S0006-3495(86)83622-0.

On the attribution and additivity of binding energies.关于结合能的归因和可加性。

Proc Natl Acad Sci U S A. 1981 Jul;78(7):4046-50. doi: 10.1073/pnas.78.7.4046.

Cross-linking of myosin subfragment 1. Nucleotide-enhanced modification by a variety of bifunctional reagents.

J Biol Chem. 1980 Dec 10;255(23):11135-40.

A new model for the geometry of the binding of myosin crossbridges to muscle thin filaments.肌球蛋白横桥与肌肉细肌丝结合的几何结构新模型。

J Mol Biol. 1981 Apr 5;147(2):297-324. doi: 10.1016/0022-2836(81)90442-3.

Angles of nucleotides bound to cross-bridges in glycerinated muscle fiber at various concentrations of epsilon-ATP, epsilon-ADP and epsilon-AMPPNP detected by polarized fluorescence.通过偏振荧光检测在不同浓度的ε-ATP、ε-ADP和ε-AMPPNP下甘油化肌纤维中与横桥结合的核苷酸的角度。

J Mol Biol. 1981 Mar 15;146(4):539-60. doi: 10.1016/0022-2836(81)90046-2.

Correlation of DNA exonic regions with protein structural units in haemoglobin.血红蛋白中DNA外显子区域与蛋白质结构单元的相关性。

Nature. 1981 May 7;291(5810):90-2. doi: 10.1038/291090a0.

Structural evidence that myosin heads may interact with two sites on F-actin.肌球蛋白头部可能与F-肌动蛋白上的两个位点相互作用的结构证据。

Nature. 1982 Sep 30;299(5882):467-9. doi: 10.1038/299467a0.

Three-dimensional reconstruction of thin filaments decorated with a Ca2+-regulated myosin.用钙离子调节的肌球蛋白修饰的细肌丝的三维重建

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Protein folding.蛋白质折叠

Annu Rev Biochem. 1981;50:497-532. doi: 10.1146/annurev.bi.50.070181.002433.

Relation between structure and function of alpha/beta-proteins.α/β 蛋白的结构与功能之间的关系。

Q Rev Biophys. 1980 Aug;13(3):317-38. doi: 10.1017/s0033583500001712.

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