title: Diffraction ellipsometry studies of osmotically compressed muscle fibers.
abstract: Microstructural features of relaxed, skinned muscle fibers compressed with polyvinylpyrrolidone were examined by optical diffraction ellipsometry. This technique is sensitive to the optical anisotropy within the muscle, including that due to intrinsic properties of the protein molecules as well as that due to the regular arrangement of proteins in the surrounding medium. The change in polarization state of light after interacting with the muscle is described by the differential field ratio (DFR) and birefringence (delta n). Compression of single fibers (sarcomere length = 2.6 microns) with 0%-21% polyvinylpyrrolidone caused an increase of up to 23% and 31% for DFR and delta n, respectively. The largest increase in both parameters occurred at intermediate sarcomere lengths. Theoretical modelling of the results suggest that the average S-1 tilt angle may be reduced upon compression of the filament lattice. This is supported by experiments in which S-1 was enzymatically cleaved with alpha-chymotrypsin. Separate experiments comparing fibers with intact membranes and skinned fibers compressed to an equivalent lattice spacing showed little difference in DFR or delta n.
authors: Graduate Group in Biophysics, University of California, Davis 95616.
authors: W L
authors: WL
authors: Kerr
authors: R J
authors: RJ
authors: Baskin
authors: Y
authors: Y
authors: Yeh
mesh_terms: D000818:Animals; D001718:Birefringence; D009132:Muscles / Q000166:cytology / Q000502:physiology* / Q000648:ultrastructure; D015879:Myosin Subfragments / Q000737:chemistry / Q000502:physiology; D009904:Optical Rotation; D009997:Osmotic Pressure; D011894:Rana pipiens; D012518:Sarcomeres / Q000502:physiology / Q000648:ultrastructure; D014961:X-Ray Diffraction
chemical_list: D015879:Myosin Subfragments