Analysis of nucleotide myosin complexes in skeletal muscle fibres by DSC and EPR

Journal of Biochemical and Biophysical Methods

Volumn 53, Issue 1-3, 2002, Pages 75-87

  Lorinczy, D ^a,b   Hartvig, N ^a   Belagyi, J ^a  

^a UNIVERSITY OF PÉCS   (Hungary)

^b Fax: +36 72 536 261 ^*  (Hungary)

Author keywords

ADP state; DSC; EPR; Intermediate states; Unfolding of myosin

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ALUMINUM FLUORIDE; BERYLLIUM; GLYCEROL; MYOSIN; NUCLEOTIDE; ORTHOVANADIC ACID; ALUMINUM DERIVATIVE; FLUORIDE; MOLECULAR MOTOR; PHOSPHORUS; VANADIC ACID;

ANIMAL TISSUE; CALORIMETRY; CONFERENCE PAPER; CONTROLLED STUDY; DEVICE; DIFFERENTIAL SCANNING CALORIMETRY; ELECTRON SPIN RESONANCE; ENTHALPY; HYDROLYSIS; MELTING POINT; MUSCLE RIGIDITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; SIMULATION; SKELETAL MUSCLE; SPIN LABELING; TEMPERATURE DEPENDENCE; THERMAL ANALYSIS; ANIMAL; ARTICLE; CHEMISTRY; COMPARATIVE STUDY; GENETIC PROCEDURES; HEAT; IN VITRO STUDY; KINETICS; MACROMOLECULE; METABOLISM; METHODOLOGY; MUSCLE CELL; PROTEIN DENATURATION; PSOAS MUSCLE; RAT; TEMPERATURE;

ORYCTOLAGUS CUNICULUS;

ACTINS; ALUMINUM COMPOUNDS; ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; ELECTRON SPIN RESONANCE SPECTROSCOPY; FLUORIDES; HEAT; KINETICS; MACROMOLECULAR SUBSTANCES; MOLECULAR MOTOR PROTEINS; MOLECULAR PROBE TECHNIQUES; MUSCLE FIBERS; MYOSINS; NUCLEOTIDES; PHOSPHORUS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PSOAS MUSCLES; RATS; TEMPERATURE; VANADATES;

EID: 0036803318     PISSN: 0165022X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-022X(02)00095-7     Document Type: Conference Paper

References (23)

1. Eisenberg E., Greene L.E. The relation of muscle biochemistry to muscle physiology. Annu. Rev. Physiol. 42:1980;293-309.
2. Brenner B., Eisenberg E. Jacob R., Just H.J., Holubarsch Ch. Cardiac energetics basic mechanisms and clinical applications. Supplement to basic research in cardiology. vol. 82.2:1987;3-16 Springer-Verlag, New York.
3. Rayment I., Holden H.M., Whittaker M., Yohn C.B., Lorenz M., Holmes K.C.et al. Structure of the actin-myosin complex and its implications for muscle contraction. Science. 261:1993;58-65.
4. Rayment I., Holden H.M. The three-dimensional structure of a molecular motor. TIBS. 19:1994;129-134.
5. Janmey P.A., Hvidt S., Oster G.F., Lamb J., Stossel T.P., Hartwig J.H. Effect of ATP on actin filament stiffness. Nature. 347:1990;95-99.
6. Orlova A., Egelman E.H. Structural dynamics of F-actin: I. Changes in the C terminus. J. Mol. Biol. 245:1995;582-597.
7. Trayer J.P., Trayer H.R., Levine B.A. Evidence that the N-terminal region of A1-light chain of myosin interacts directly with the C-terminal region of actin. Eur. J. Biochem. 164:1987;259-266.
8. Franks-Skiba K., Cooke R. The conformation of the active site of myosin probed using mant-nucleotides. Biophys. J. 68:1995;142S-147S.
9. Fisher A.J., Smith C.A., Thoden J., Smith R., Sutoh K., Holden H.M.et al. Structural studies of myosin:nucleotide complexes: a revised model for the molecular basis of muscle contraction. Biophys. J. 68:1995;19S-28S.
10. Smith C.A., Rayment I. X-ray structure of the magnesium (II) ADP vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry. 35:1996;5404-5417.
11. Fajer P.G., Fajer E.A., Matta J.J., Thomas D.D. Effect of ADP on the orientation of spin-labeled myosin heads in muscle fibres: a high-resolution study with deuterated spin labels. Biochemistry. 29:1990;5865-5871.
12. Raucher D., Sár C.P., Hideg K., Fajer P.G. Myosin catalytic domain flexibility in MgADP. Biochemistry. 33:1994;14317-14323.
13. Ajtai K., Ringler A., Burghardt T.P. Probing cross-bridge angular transitions using multiple extrinsic reporter groups. Biochemistry. 31:1992;207-217.
14. Lymn R.W., Taylor E.W. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry. 10:1971;4617-4624.
15. Taylor E.W. Mechanism of actomyosin ATPase and the problem of muscle contraction. CRC Crit. Rev. Biochem. 6:1979;103-164.
16. Geeves M.A. The dynamics of actin and myosin association and the crossbridge model of muscle contraction. Biochem. J. 274:1991;1-14.
17. Zhao L., Naber N., Cooke R. Muscle cross-bridges bound to actin are disordered in the presence of 2,3-butanedione monoxime. Biophys. J. 68:1995;1980-1990.
18. Thomas D.D., Cooke R. Orientation of spin-labeled myosin heads in glycerinated muscle fibres. Biophys. J. 32:1980;891-906.
19. Belagyi J., Lorinczy D. Internal motion in myosin head: effect of ADP and ATP. Biochem. Biophys. Res. Commun. 219:1996;936-940.
20. Belagyi J., Frey I., Pótó L. ADP-induced changes in ordering of spin-labelled myosin heads in muscle fibres. Eur. J. Biochem. 224:1994;215-222.
21. Fajer P.G., Marsh D. Microwave and modulation field inhomogeneities and effect of cavity Q in saturation transfer EPR spectra. Dependence of sample size. J. Magn. Res. 49:1982;212-224.
22. Lorinczi D., Hoffmann U., Pótó L., Belagyi J., Laggner P. Conformational changes in bovine heart myosin as studied by EPR and DSC techniques. Gen. Physiol. Biophys. 9:1990;589-603.
23. Raucher D., Fajer P.G. Orientation and dynamics of myosin heads in aluminium fluoride induced pre-power stroke states: an EPR study. Biochemistry. 33:1994;11993-11999.