PROXIMITY RELATIONSHIPS AMONG MUSCLE PROTEINS

肌肉蛋白质之间的邻近关系

• 批准号: 2078514
• 负责人: Terence Tao
• 金额: $ 29.56万
• 依托单位: BOSTON BIOMEDICAL RESEARCH INSTITUTE
• 依托单位国家: 美国
• 财政年份: 1979
• 资助国家: 美国
• 起止时间: 1979-08-01 至 1996-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2078514
• 关键词: actins; bioenergetics; calcium; chemical binding; circular dichroism; conformation; crosslink; cytoskeletal proteins; fluorescence polarization; fluorescence spectrometry; fluorescent dye /probe; intermolecular interaction; laboratory rabbit; microfilaments; molecular site; muscle contraction; mutant; myosins; photosensitizing agents; protein engineering; protein purification; protein structure function; recombinant DNA; site directed mutagenesis; striated muscles; tropomyosin; troponin

The long-term objective of this project is to elucidate the mechanisms for 1) transduction of energy during contraction of skeletal muscle, 2) the regulation of skeletal muscle contraction by calcium ions. Since these two processes are fundamental to the functioning of normal muscle tissue, this work may provide insight into the nature of pathological muscle conditions. This objective will be achieved by determining the spatial relationships among the four major contractile proteins: myosin, actin, tropomyosin and troponin. Furthermore, how these spatial relationships change with the functional state of muscle (relaxed, activated, or in rigor) will be examined. Information so derived will be used to reconstruct the molecular events that occur during muscle contraction and its regulation. Principally, two techniques will be used to determine spatial relationships: excitation energy transfer, and photochemical crosslinking. The distances between sites in tropomyosin and in the three subunits of troponin will be determined by excitation energy transfer measurements. Simultaneously, amino acid residues at the interfaces between the proteins will be identified using photocrosslinking and peptide analysis techniques. Information derived from these studies will be used to construct a three-dimensional model for the troponin.tropomyosin complex. In a similar fashion, distances between sites in tropomyosin, actin and myosin will be determined, and the interaction interfaces between these proteins identified. This will yield information on the location of tropomyosin in the myosin.actin.tropomyosin complex, and the contact region between myosin and actin.

该项目的长期目标是阐明的机制