Mechanical Coupling between Myosin Molecules Causes Differences between Ensemble and Single-Molecule Measurements
نویسندگان
چکیده
منابع مشابه
Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.
In contracting muscle, individual myosin molecules function as part of a large ensemble, hydrolyzing ATP to power the relative sliding of actin filaments. The technological advances that have enabled direct observation and manipulation of single molecules, including recent experiments that have explored myosin's force-dependent properties, provide detailed insight into the kinetics of myosin's ...
متن کاملInformation For “ Mechanical coupling between myosin molecules causes differences between ensemble and single molecule measurements ”
We consider the 4-state model for actomyosin interaction shown in Fig. 1 of the main text and reproduced here below (see Fig. 1). Briefly, unbound (or weakly-bound) myosin with ADP and phosphate (Pi) in its active site transitions to a state where it strongly binds to actin. We label the former state (un-/weaklybound with ADP and Pi in the active site) state 1, while the latter state (bound wit...
متن کاملDirect Measurements of Local Coupling between Myosin Molecules Are Consistent with a Model of Muscle Activation
Muscle contracts due to ATP-dependent interactions of myosin motors with thin filaments composed of the proteins actin, troponin, and tropomyosin. Contraction is initiated when calcium binds to troponin, which changes conformation and displaces tropomyosin, a filamentous protein that wraps around the actin filament, thereby exposing myosin binding sites on actin. Myosin motors interact with eac...
متن کاملStrong coupling between a metallic nanoparticle and a single molecule
We theoretically investigate the strong coupling between a single molecule and a single metallic nanoparticle. A theory suited for the quantum-mechanical description of surface plasmon polaritons SPPs is developed. The coupling between these SPPs and a single molecule, and the modified molecular dynamics in the presence of the nanoparticle are described within a combined Drude and boundary-elem...
متن کاملMuscle, myosin and single molecules.
Whereas we have a great deal of information about myosin, there remain fundamental questions about its mechanism (and those of other motor proteins). Single-molecule technologies enable us to make measurements we cannot make from large ensembles of molecules. Optical tweezers (and similar techniques) are used to measure the mechanical aspects of actomyosin interactions, including force, displac...
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: Biophysical Journal
سال: 2012
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2012.06.031