CHEMISTRY OF MUSCLE PROTEINS

肌肉蛋白质的化学性质

• 批准号: 3151057
• 负责人: SUSAN LOWEY
• 金额: $ 18.38万
• 依托单位: BRANDEIS UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1976
• 资助国家: 美国
• 起止时间: 1976-01-01 至 1985-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3151057
• 关键词: X ray crystallography; calcium; chemical binding; chemical fingerprinting; chemical group; chemical structure function; crystallization; electron microscopy; embryo /fetus; fluorescent dye /probe; immunochemistry; isozymes; monoclonal antibody; muscle contraction; muscle relaxation; myofibrils; myogenesis; nucleotides; phosphorylation; saltwater environment; smooth muscle

A major aim in our research is to discover the role of the low molecular weight subunits in myosin. After nearly a decade of effort by several laboratories, their function in vertebrate skeletal muscle remains obscure. One assumes that they are probably involved in the basic actomyosin interaction, but little firm evidence is available to support this hypothesis. We will pursue two main directions to advance this problem: (1) We will attempt to localize the two classes of light chains in the myosin head by introducing specific markers, such as fluorescent probes or monoclonal antibodies into defined sites on the light and heavy chain subunits. Distances between fluorophores will be measured by Forster energy transfer. Antibody-myosin complexes will be viewed by electron microscopy of shadow-cast preparations. (2) We will compare the functional and structural properties of several isoenzymes of myosin, among them fast and slow myosins, embryonic myosin from several stages of development, and synthetic hybrids formed by combining the subunits of slow and fast myosins. Techniques will include kinetic analysis, two-dimensional peptide mapping, and immunological identification of common sequences. By studying these myosin polymorphs both in the monomeric and filamentous state, we hope to gain additional insights into how the myosin molecule works, and why muscle is composed of such a mosaic of different fiber types.

我们研究的一个主要目的是发现低分子量的作用 肌球蛋白中的亚基。 经过多个实验室近十年的努力， 它们在脊椎动物骨骼肌中的功能仍然不清楚。 有人假设 它们可能参与基本的肌动球蛋白相互作用，但很少有证据表明 有证据支持这一假设。 我们将追求两个主要目标 推进这个问题的方向：（1）我们将尝试本地化这两个 通过引入特定标记来区分肌球蛋白头部的轻链类别，例如 作为荧光探针或单克隆抗体进入光的指定位点 和重链亚基。 荧光团之间的距离将通过以下方式测量 福斯特能量转移。 抗体-肌球蛋白复合物将通过电子观察 阴影投射制剂的显微镜检查。 (2)我们将比较功能和 几种肌球蛋白同工酶的结构特性，其中包括快的和慢的 肌球蛋白、来自多个发育阶段的胚胎肌球蛋白以及合成的 由慢肌球蛋白和快肌球蛋白的亚基组合而成的杂种。 技巧 将包括动力学分析、二维肽图谱和 共同序列的免疫学鉴定。 通过研究这些肌球蛋白 单体和丝状多晶型物，我们希望获得 关于肌球蛋白分子如何工作以及为什么肌肉是这样的更多见解 由不同类型的纤维镶嵌而成。

项目成果

Isolated and distribution of myosin isoenzymes in chicken pectoralis muscle.

鸡胸肌肌球蛋白同工酶的分离和分布。

• DOI: 10.1016/0022-2836(81)90510-6
• 发表时间: 1981
• 期刊: Journal of molecular biology
• 影响因子: 5.6
• 作者: Silberstein,L;Lowey,S
• 通讯作者: Lowey,S

Conformational states of smooth muscle myosin. Effects of light chain phosphorylation and ionic strength.

平滑肌肌球蛋白的构象状态。

• 发表时间: 1984
• 期刊: The Journal of biological chemistry
• 作者: Trybus,KM;Lowey,S
• 通讯作者: Lowey,S

Mechanism of smooth muscle myosin phosphorylation.

平滑肌肌球蛋白磷酸化机制。

• 发表时间: 1985
• 期刊: The Journal of biological chemistry
• 作者: Trybus,KM;Lowey,S
• 通讯作者: Lowey,S

Crystallization of myosin subfragment 1.

肌球蛋白亚片段1的结晶。

• DOI: 10.1073/pnas.81.14.4378
• 发表时间: 1984
• 期刊: Proceedings of the National Academy of Sciences of the United States of America
• 影响因子: 11.1
• 作者: Rayment,I;Winkelmann,DA
• 通讯作者: Winkelmann,DA

Myosin subunit interactions. Localization of the alkali light chains.

肌球蛋白亚基相互作用。

• 发表时间: 1985
• 期刊: The Journal of biological chemistry
• 作者: Waller,GS;Lowey,S
• 通讯作者: Lowey,S