Abstract
A fluorescence depolarization study of the orientational distribution of crossbridges in dye-labelled muscle fibres is presented. The characterization of this distribution is important since the rotation of crossbridges is a key element in the theory of muscle contraction. In this study we exploited the advantages of angle-resolved experiments to characterize the principal features of the orientational distribution of the crossbridges in the muscle fibre. The directions of the transition dipole moments in the frame of the dye and the orientation and motion of the dye relative to the crossbridge determined previously were explicitly incorporated into the analysis of the experimental data. This afforded the unequivocal determination of all the second and fourth rank order parameters. Moreover, this additional information provided discrimination between different models for the orientational behaviour of the crossbridges. Our results indicate that no change of orientation takes place upon a transition from rigor to relaxation. The experiments, however, do no rule out a conformational change of the myosin S1 during the transition.
MeSH Terms
Animals
Fluorescent Dyes
Models, Biological
Models, Theoretical
Muscle Contraction
Muscle Fibers, Skeletal/physiology,ultrastructure
Muscle, Skeletal/physiology,ultrastructure
Naphthalenesulfonates
Rabbits
Scattering, Radiation
Spectrometry, Fluorescence
Chemicals
Fluorescent Dyes
Naphthalenesulfonates
1,5-I-AEDANS
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
van der Heide U A
Debye Institute, Department of Molecular Biophysics, University of Utrecht, Buys Ballot Laboratory, The Netherlands.
Rem O E
Gerritsen H C
de Beer E L
Schiereck P
Trayer I P
Levine Y K
References (30)
30 references, click to expand
-
Pollard to actomyosin: "freeze! Don't even move your head".
Biophys J. 1993 Feb;64(2):297-8
PMID: 8384499
-
Direct visualization by electron microscopy of the weakly bound intermediates in the actomyosin adenosine triphosphatase cycle.
Biophys J. 1993 Feb;64(2):454-71
PMID: 8457671
-
Three-dimensional structure of myosin subfragment-1: a molecular motor.
Science. 1993 Jul 2;261(5117):50-8
PMID: 8316857
-
Cross-bridge orientation in skeletal muscle measured by linear dichroism of an extrinsic chromophore.
J Mol Biol. 1982 Jul 5;158(3):391-414
PMID: 6982344
-
Orientation and mobility of molecules in membranes studied by polarized light spectroscopy.
Q Rev Biophys. 1980 Feb;13(1):63-118
PMID: 7012891
-
Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells.
J Physiol (Paris). 1979;75(5):463-505
PMID: 533865
-
Evidence for cross-bridge attachment in relaxed muscle at low ionic strength.
Proc Natl Acad Sci U S A. 1982 Dec;79(23):7288-91
PMID: 6961408
-
The mechanism of muscle contraction.
CRC Crit Rev Biochem. 1986;21(1):53-118
PMID: 3524992
-
Tension development and calcium sensitivity in skinned muscle fibres of the frog.
Pflugers Arch. 1985 Sep;405(1):19-23
PMID: 2414721
-
The double array of filaments in cross-striated muscle.
J Biophys Biochem Cytol. 1957 Sep 25;3(5):631-48
PMID: 13475381
-
Reciprocal reactivities of specific thiols when actin binds to myosin.
Proc Natl Acad Sci U S A. 1976 Feb;73(2):302-6
PMID: 1061133
-
Caffeine suppresses length dependency of Ca2+ sensitivity of skinned striated muscle.
Am J Physiol. 1988 Apr;254(4 Pt 1):C491-7
PMID: 3354648
-
Proposed mechanism of force generation in striated muscle.
Nature. 1971 Oct 22;233(5321):533-8
PMID: 4939977
-
Muscle structure and theories of contraction.
Prog Biophys Biophys Chem. 1957;7:255-318
PMID: 13485191
-
Atomic model of the actin filament.
Nature. 1990 Sep 6;347(6288):44-9
PMID: 2395461
-
Observation of two orientations from rigor cross-bridges in glycerinated muscle fibers.
Biochemistry. 1986 Oct 7;25(20):6203-7
PMID: 3790516
-
Transients in orientation of a fluorescent cross-bridge probe following photolysis of caged nucleotides in skeletal muscle fibres.
J Mol Biol. 1992 Jan 5;223(1):185-203
PMID: 1530978
-
The mechanism of muscular contraction.
Science. 1969 Jun 20;164(3886):1356-65
PMID: 4181952
-
Mapping global angular transitions of proteins in assemblies using multiple extrinsic reporter groups.
Biochemistry. 1992 Jan 14;31(1):200-6
PMID: 1310030
-
Probing cross-bridge angular transitions using multiple extrinsic reporter groups.
Biochemistry. 1992 Jan 14;31(1):207-17
PMID: 1310031
-
The orientation of transition moments of dye molecules used in fluorescence studies of muscle systems.
Eur Biophys J. 1992;21(4):263-72
PMID: 1385106
-
Polarization of fluorescence from single skinned glycerinated rabbit psoas fibers in rigor and relaxation.
Biochim Biophys Acta. 1977 Mar 11;459(3):578-95
PMID: 849438
-
Spectroscopic probes of muscle cross-bridge rotation.
Annu Rev Physiol. 1987;49:691-709
PMID: 3032079
-
Atomic structure of the actin:DNase I complex.
Nature. 1990 Sep 6;347(6288):37-44
PMID: 2395459
-
Angle of active site of myosin heads in contracting muscle during sudden length changes.
J Muscle Res Cell Motil. 1985 Feb;6(1):43-52
PMID: 4008630
-
Microsecond rotational dynamics of phosphorescent-labeled muscle cross-bridges.
Biochemistry. 1988 May 3;27(9):3343-51
PMID: 2455541
-
Force and force transients in skeletal muscle fibres of the frog skinned by freeze-drying.
Pflugers Arch. 1983 Jun 1;397(4):272-6
PMID: 6412211
-
Time-resolved rotational dynamics of phosphorescent-labeled myosin heads in contracting muscle fibers.
Biochemistry. 1990 Oct 30;29(43):10023-31
PMID: 1703000
-
A comparison of order and orientation of crossbridges in rigor and relaxed muscle fibres using fluorescence polarization.
J Muscle Res Cell Motil. 1983 Dec;4(6):671-93
PMID: 6668358
-
Structure of the actin-myosin complex and its implications for muscle contraction.
Science. 1993 Jul 2;261(5117):58-65
PMID: 8316858