Probes bound to myosin Cys-707 rotate during length transients in contraction
نویسندگان
چکیده
منابع مشابه
Probes bound to myosin Cys-707 rotate during length transients in contraction.
It is widely conjectured that muscle shortens because portions of myosin molecules (the "cross-bridges") impel the actin filament to which they transiently attach and that the impulses result from rotation of the cross-bridges. Crystallography indicates that a cross-bridge is articulated-consisting of a globular catalytic/actin-binding domain and a long lever arm that may rotate. Conveniently, ...
متن کاملContraction after small transients
Contraction theory is a powerful tool for proving asymptotic properties of nonlinear dynamical systems including convergence to an attractor and entrainment to a periodic excitation. We consider three generalizations of contraction with respect to a norm that allow contraction to take place after small transients in time and/or amplitude. These generalized contractive systems (GCSs) are useful ...
متن کاملFluctuations in polarized fluorescence: evidence that muscle cross bridges rotate repetitively during contraction.
Particular thiols of the myosin subfragment 1 moieties of single glycerinated muscle fibers are covalently labeled with rhodamine. By using appropriate solutions such fibers can be relaxed, be in rigor, or develop active isometric tension. The rhodamine is excited by polarized 514.5-nm laser light; the greater than 580-nm fluorescence is resolved into orthogonal components and the intensity of ...
متن کاملThe mechanism of force generation in myosin: a disorder-to-order transition, coupled to internal structural changes.
We propose a molecular mechanism of force generation in muscle, based primarily on site-specific spectroscopic probe studies of myosin heads in contracting muscle fibers and myofibrils. Electron paramagnetic resonance (EPR) and time-resolved phosphorescence anisotropy (TPA) of probes attached to SH1 (Cys 707, in the catalytic domain of the head) have consistently shown that most myosin heads in...
متن کاملChange in the reactivity of myosin during muscle contraction.
Myosin can be labeled with 1 -fluoro-2,4-dinitrobenzene in frog muscle. The incorporation into myosin is decreased during isotonic contraction. In contrast no difference is found in the incorporation into the sarcoplasmic proteins of contracting and resting muscle. Myosin also reacts with iodoacetate in frog muscle. However, this reaction does not depend on the functional state of the muscle. T...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1997
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.94.18.9631