期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2002
卷号：99
期号：23
页码：14801-14806
DOI：10.1073/pnas.232161999
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：We have used luminescence resonance energy transfer between regulatory light chains (RLC) to detect structural changes within the dimeric myosin molecule in contracting muscle fibers. Fully functional scallop muscle fibers were prepared such that each myosin molecule contained a terbium-labeled (luminescent donor) RLC on one head and a rhodamine-labeled (acceptor) RLC on the other. Time-resolved luminescence energy transfer between the two heads increased upon the transition from relaxation (ATP) to contraction (ATP plus Ca) and increased further in rigor (no ATP). Combined with experiments on mutant RLCs labeled specifically at other sites, these results support a model in which the force-generating weak-to-strong transition causes one myosin LC domain to tilt through a 30{degrees} angle toward the other, thus acting as a coordinated lever arm.
