title: Photon correlation spectroscopy of the polarization signal from single muscle fibres.
abstract: Measurements of crossbridge dynamics have been obtained from the spectrum of diffracted light derived from single, skinned fibres of skeletal muscle. This technique combines optical ellipsometry with photon correlation spectroscopy of the intrinsic reporters from the muscle cell. The difference in the intensities of the two linearly polarized electric field components of diffracted light is autocorrelated in time, and the dynamics of optical anisotropy from the contributing units of the sarcomere are measured. In focusing on the fast-time dynamics, we detected two principal features: a rapidly relaxing temporal signal with a relaxation time of approximately 5 microseconds, and an oscillatory component which transforms into a broad but spectrally defined signal centred at around 370 kHz. Experiments were conducted to measure changes of these two signals upon relax-rigor transition and alpha-chymotrypsin degradation. These studies strongly suggest that the relaxational component of the signal is primarily due to myosin crossbridge motion; the 370 kHz spectral signal has as its likely source the myosin thick filament.
authors.affiliation: Department of Applied Science, University of California, Davis 95616.
authors.forename: Y
authors.initials: Y
authors.lastname: Yeh
authors.forename: R J
authors.initials: RJ
authors.lastname: Baskin
authors.forename: S
authors.initials: S
authors.lastname: Shen
authors.forename: M
authors.initials: M
authors.lastname: Jones
mesh_terms: D000818:Animals; D002918:Chymotrypsin; D009119:Muscle Contraction / Q000502:physiology*; D009126:Muscle Relaxation / Q000502:physiology; D009132:Muscles / Q000032:analysis*; D011827:Radiation; D011894:Rana pipiens; D013057:Spectrum Analysis / Q000379:methods
chemical_list: D002918:Chymotrypsin