BIOPHYSICAL CHEMICAL STUDIES OF MUSCLE PROTEINS

肌肉蛋白的生物物理化学研究

• 批准号: 3150708
• 负责人: William J Harrington
• 金额: $ 33.64万
• 依托单位: JOHNS HOPKINS UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1977
• 资助国家: 美国
• 起止时间: 1977-09-01 至 1987-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3150708
• 关键词: adenosinetriphosphatase; calcium; conformation; crosslink; density gradient ultracentrifugation; electron microscopy; fluorescence spectrometry; gel electrophoresis; hydrolysis; immunochemistry; ionic strengths; magnesium; molecular rearrangement; molecular weight; muscle contraction; muscle proteins; myofibrils; optical rotation; polymerization; reagent /indicator; sarcomeres; striated muscles; thermodynamics; viscosity

We plan to continue our studies on the radial disposition of the cross-bridges of thick filaments in glycerinated muscle using bifunctional cross-linking reagents and proteolytic enzymes to probe release of the cross-bridges from the thick filament surface. We will also continue our current experiments on the tritium exchange of glycerinated muscle fibers under activating and resting conditions. The purpose of these latter experiments is to determine whether or not the LMM-HMM hinge region of the myosin molecule undergoes a helix-coil transition during a contractile cycle thus generating the contractile force. We hope to establish the size and location of the segment involved in the proposed force-generating process by isolation of the labelled segment following the tritium exchange reaction. We will continue our experiments on the number of myosin molecules in the native thick filament of skeletal muscle using the Scanning Transmission Electron Microscope (STEM). This work is being carried out in collaboration with Dr. Michael Beer and his group. We are continuing our comparative studies on the thermal melting behaviors of the long S-2 subfragments isolated from frog and rabbit myosins with a view to determining whether the physiological working temperature of the muscle is reflected in the thermal stability of the LMM-HMM hinge region.

我们计划继续研究跨桥的径向布置。 利用双功能交联剂制备甘油肌肉中的粗丝 试剂和蛋白水解酶来探测交叉桥的释放 较厚的细丝表面。我们还将继续目前的实验， 甘油化肌纤维在激活和静息状态下的氚交换 条件。后面这些实验的目的是确定是否或 而不是肌球蛋白分子的1 mm-mm铰链区经历螺旋卷曲 在收缩周期中的过渡，从而产生收缩力。我们 希望确定建议中涉及的部分的大小和位置 通过分离紧跟在 氚交换反应。 我们将继续对天然肌球蛋白分子的数量进行实验 用扫描透射法研究骨骼肌粗纤维 显微镜(STEM)。这项工作是与Dr. 迈克尔·比尔和他的团队。 我们正在继续进行关于热熔化行为的比较研究 从蛙和兔肌球蛋白中分离出S-2长亚段以期 确定肌肉的生理工作温度是否为 反映在LMM-HMM铰链区的热稳定性上。

项目成果

Measurement of the fraction of myosin heads bound to actin in rabbit skeletal myofibrils in rigor.

测量兔骨骼肌原纤维中与肌动蛋白结合的肌球蛋白头部的分数。

• DOI: 10.1016/0022-2836(81)90352-1
• 发表时间: 1981
• 期刊: Journal of molecular biology
• 影响因子: 5.6
• 作者: Lovell,SJ;Harrington,WF
• 通讯作者: Harrington,WF

Cross-bridge movement in muscle and the conformation of the myosin hinge.

肌肉的跨桥运动和肌球蛋白铰链的构象。

• DOI: 10.1002/9780470720752.ch11
• 发表时间: 1983
• 期刊: Ciba Foundation symposium
• 作者: Harrington,WF;Ueno,H;Tsong,TY
• 通讯作者: Tsong,TY

An enzyme-probe method to detect structural changes in the myosin rod.

检测肌球蛋白杆结构变化的酶探针方法。

• DOI: 10.1016/0022-2836(84)90402-9
• 发表时间: 1984
• 期刊: Journal of molecular biology
• 影响因子: 5.6
• 作者: Ueno,H;Harrington,WF
• 通讯作者: Harrington,WF

Assembly processes in vertebrate skeletal thick filament formation.

脊椎动物骨骼粗丝形成的组装过程。

• DOI: 10.1146/annurev.bb.17.060188.001245
• 发表时间: 1988
• 期刊: Annual review of biophysics and biophysical chemistry
• 作者: Davis,JS

Cross-linking within the thick filaments of muscle and its effect on contractile force.

肌肉粗丝内的交联及其对收缩力的影响。

• DOI: 10.1021/bi00386a051
• 发表时间: 1987
• 期刊: Biochemistry
• 影响因子: 2.9
• 作者: Ueno,H;Harrington,WF
• 通讯作者: Harrington,WF