Some Useful References

Abrahams, J. P., Leslie, A. G., Lutter, R. & Walker, J. E. (1994). The structure of F1-ATPase from bovine heart mitochondria determined at 2.8Å resolution. Nature 370, 621-628.

Anson, M., Geeves, M. A., Kurzawa, S. E. & Manstein, D. J. (1996). Myosin motors with artificial lever arms. Embo Journal 15(22), 6069-74.

Bagshaw, C. R. & Trentham, D. R. (1973). The reversibility of adenosine triphosphate cleavage by myosin. Biochemical Journal 133(2), 323-8.

Bagshaw, C. R., Trentham, D. R., Wolcott, R. G. & Boyer, P. D. (1975). Oxygen exchange in the gamma-phosphoryl group of protein-bound ATP during Mg2+-dependent adenosine triphosphatase activity of myosin. Proceedings of the National Academy of Sciences of the United States of America 72(7), 2592-6.

Bohm, A., Gaudet, R. & Sigler, P. B. (1997). Structural aspects of heterotrimeric G-protein signaling. [Review] [52 refs]. Current Opinion in Biotechnology 8(4), 480-7.

Burghardt, T. P., Garamszegi, S. P., Park, S. & Ajtai, K. (1998). Tertiary structural changes in the cleft containing the ATP sensitive tryptophan and reactive thiol are consistent with pivoting of the myosin heavy chain at Gly699. Biochemistry 37(22), 8035-47.

Coates, J. H., Criddle, A. H. & Geeves, M. A. (1985). Pressure-relaxation studies of pyrene-labelled actin and myosin subfragment 1 from rabbit skeletal muscle. Evidence for two states of acto-subfragment 1. Biochemical Journal 232(2), 351-6.

Coluccio, L. M., Veigel, C., White, D. & Molloy, J. E. (1998). Biophys. J. 74, A225.

Cooke, R. (1986). The Mechanism of Muscle Contraction. CRC Crit Rev. Biochem 21, 53-118.

Cope, T. V., Whisstock, J., Rayment, I. & Kendrick-Jones, J. (1996). Conservation within the myosin motor domain: implications for structure and function. Structure 4, 969-987.

Corrie, J. E. T., Brandmeier, B. D., Ferguson, R. E., Trentham, D. R., Kendrick-Jones, J., Hopkins, S. C., van der Heide, U. A., Goldman, Y. E., Sabido-David, C., Dale, R. E., Criddle, S. & Irving, M. (1999). Dynamic measurement of conformational changes of proteins in their native environment: tilt and twist of the myosin light chain domain in muscle contraction. Nature 400, 425-430

Cremo, C. R. & Geeves, M. A. (1998). Interaction of actin and ADP with the head domain of smooth muscle myosin: implications for strain-dependent ADP release in smooth muscle. Biochemistry 37(7), 1969-78.

Dale, M. P. & Hackney, D. D. (1987). Analysis of positional isotope exchange in ATP by cleavage of the beta P-O gamma P bond. Demonstration of negligible positional isotope exchange by myosin. Biochemistry 26(25), 8365-72.

Dominguez, R., Freyzon, Y., Trybus, K. M. & Cohen, C. (1998). Crystal structure of a verterbrate smooth muscle motor domain and its complex with the essential light chain: visualisation of the pre-power stroke state. Cell 94(5), 559-571.

Esnouf, R. M. (1997). J. Mol. Graphics 15, 132-134.

Fisher, A. J., Smith, C. A., Thoden, J. B., Smith, R., Sutoh, K., Holden, H. M. & Rayment, I. (1995). X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. Biochemistry 34(28), 8960-72.

Fortune, N. S., Geeves, M. A. & Ranatunga, K. W. (1991). Tension responses to rapid pressure release in glycerinated rabbit muscle fibers. Proceedings of the National Academy of Sciences of the United States of America 88(16), 7323-7.

Geeves, M. A. (1989). Dynamic interaction between actin and myosin subfragment 1 in the presence of ADP. Biochemistry 28(14), 5864-71.

Geeves, M. A. (1991). The influence of pressure on actin and myosin interactions in solution and in single muscle fibres. [Review] [26 refs]. Journal of Cell Science Supplement 14, 31-5.

Geeves, M. A. (1992). The actomyosin ATPase: a two-state system. [Review] [36 refs]. Philosophical Transactions of the Royal Society of London Series B: Biological Sciences 336(1276), 63-70.

Geeves, M. A. & Conibear, P. B. (1995). The role of three-state docking of myosin S1 with actin in force generation. [Review] [28 refs]. Biophysical Journal 68(4 Suppl), 199S-201S.

Geeves, M. A., Goody, R. S. & Gutfreund, H. (1984). Kinetics of acto-S1 interaction as a guide to a model for the crossbridge cycle. Journal of Muscle Research & Cell Motility 5(4), 351-61.

Geeves, M. A. & Gutfreund, H. (1982). The use of pressure perturbations to investigate the interaction of rabbit muscle myosin subfragment 1 with actin in the presence of MgADP. Febs Letters 140(1), 11-5.

Geeves, M. A. & Holmes, K. C. (1999). Structural mechanism of muscle contraction. Ann. Rev. Biochemistry 68, 687-727.

Geeves, M. A. & Jeffries, T. E. (1988). The effect of nucleotide upon a specific isomerization of actomyosin subfragment 1. Biochemical Journal 256(1), 41-6.

Gulick, A. M., Bauer, C. B., Thoden, J. B. & Rayment, I. (1997). X-ray structures of the MgADP, MgATP ³-S, and Mg AMPPNP complexes of Dycteostelium discodium Myosin motor domain. Biochemistry 36, 11619-11628.

Holmes, K. C. (1996). Muscle proteins - their actions and interactions. Current Opinion in Structural Biology 6(6), 781-789.

Holmes, K. C. (1997). The swinging lever arm hypothesis of muscle contraction. Current Biology 7(2), R112-R118.

Holmes, K. C. and M. A. Geeves The structural basis of muscle contraction. Phil. Trans. Roy. Soc. Lond. B 355, 419-431 (2000)

Houdusse, A. & Cohen, C. (1996). Structure of the regulatory domain of scallop myosin at 2Å resolution: implications for regulation. Structure 4(1), 21-32.

Houdusse, A., Kalbokis, V. N., Himmel, D., Szent-Gyorgyi, A. G. & Cohen, C. (1999). Atomic structure of scallop myosin subfragment S1 complexed with MgADP: A novel conformation of the myosin head. Cell 97(4), 459-470.

Huston, E. E., Grammer, J. C. & Yount, R. G. (1988). Flexibility of the myosin heavy chain: direct evidence that the region containing SH1 and SH2 can move 10 A under the influence of nucleotide binding. Biochemistry 27(25), 8945-52.

Huxley, H. E. (1957). The double array of filaments in cross-striated muscle. Biophysic. and Biochem. Cytol. 3, 631-648.

Huxley, H. E. (1969). The Mechanism of Muscular Contraction. Science 164, 1356-1366.

Huxley, H. E. & Holmes, K. C. (1997). Delopment of Synchrotron Radiation as a High-intensity Source for X-ray Diffraction. Journal of Synchrotron Radiation 4(Part 6), 366-379.

Huxley, H. E., Simmons, R. M., Faruqi, A. R., Kress, M., Bordas, J. & Koch, M. H. J. (1981). Millisecond Time-Resolved changes in X-ray Reflections from Contracting Muscle during Rapid Mechanical Transients, Recorded using Synchrotron Radiation. Proc. Natl. Acad. Sci. USA 78, 2297-2301.

Irving, M., Lombardi, V., Piazzesi, G. & Ferenczi, M. A. (1992). Myosin Head Movements are Synchronous with the Elementary Force-Generating Process in Muscle. Nature (Lond.) 357, 156-158.

Irving, M., Lombardi, V., Piazzesi, G. & Ferenczi, M. A. (1992). Myosin Head Movements are Synchronous with the Elementary Force-Generating Process in Muscle. Nature (Lond.) 357, 156-158.

Irving, M., St Claire Allen, T., Sabido-David, C., Craik, J. S., Brandmeier, B., Kendrick-Jones, J., Corrie, J. E., Trentham, D. R. & Goldman, Y. E. (1995). Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle. Nature 375(6533), 688-91.

Jontes, J. D. & Milligan, R. A. (1997). Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis. Journal of Cell Biology 139(3), 683-93.

Jontes, J. D., Milligan, R. A., Pollard, T. D. & Ostap, E. M. (1997). Kinetic characterisation of brush border myosin-I ATPase. Proc. Natl. Acad. Sci. USA 94, 14332-14337.

Jontes, J. D., Wilson-Kubalek, E. M. & Milligan, R. A. (1995). The brush border myosin-1 tail swings through a 32° arc upon ADP release. Nature 378, 751-753.

Kodama, T. (1985). Thermodynamic analysis of muscle ATPase mechanisms. Physiological Reviews 65(2), 467-551.

Kuhlman, P. A. & Bagshaw, C. R. (1998). Atpase kinetics of the dictyostelium discoideum myosin ii motor domain. Journal Of Muscle Research And Cell Motility 19(5), 491-504.

Kurzawa, S. E. & Geeves, M. A. (1996). A novel stopped-flow method for measuring the affinity of actin for myosin head fragments using microgram quantities of protein. Journal of Muscle Research & Cell Motility 17, 669-76.

Kurzawa, S. E., Manstein, D. J. & Geeves, M. A. (1997). Dictyostelium discoideum myosin II: characterization of functional myosin motor fragments. Biochemistry 36(2), 317-23.

Lymn, R. W. & Taylor, E. W. (1971). Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10(25), 4617-24.

Margossian, S. S. & Lowey, S. (1973a). Substructure of the myosin molecule: III Preparation of single- headed derivatives of myosin. J. Mol. Biol. 74, 301-311.

Margossian, S. S. & Lowey, S. (1973b). Substructure of the myosin molecule; IV Interactions of myosin and its subfragments with adenosine triphosphate and actin. J. Mol. Biol. 74, 313-330.

Marston, S. B. & Taylor, E. W. (1980). Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles. Journal of Molecular Biology 139(4), 573-600.

Merritt, E. A. & Bacon, D. J. (1997). Raster3D Version 2: photorealistic molecular graphics. Methods of Enzymology 277, 505-524.

Millar, N. C., Howarth, J. V. & Gutfreund, H. (1987). A transient kinetic study of enthalpy changes during the reaction of myosin subfragment 1 with ATP. Biochemical Journal 248(3), 683-90.

Moore, P. B., Huxley, H. E. & DeRosier, D. J. (1970). Three-dimensional reconstruction of F-actin, thin filaments, and decorated thin filaments. J. Mol. Biol. 50, 279-295.

Mornet, D., Pantel, P., Audemard, E. & Kassab, R. (1979). The limited Tryptic Cleavage of Chymotriptic S1: an Approach to the Characterisation of the Actin site in Myosin Heads. Biochem. Biophys. Res. Comm. 89, 925-932.

Nicholls, A., Sharp, K. A. & Honig, B. (1991). Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.

Ostap, E. M. & Pollard, T. D. (1996). Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase. Journal of Cell Biology 132(6), 1053-60.

Pate, E., Naber, N., Matuska, M., Franks-Skiba, K. & Cooke, R. (1997). Opening of the myosin nucleotide triphosphate binding domain during the ATPase cycle. Biochemistry 36(40), 12155-66.

Rayment, I., Holden, H. M., Whittaker, M., Yohn, C. B., Lorenz, M., Holmes, K. C. & Milligan, R. A. (1993a). Structure of the actin-myosin complex and its implications for muscle contraction. Science 261(5117), 58-65.

Rayment, I., Rypniewski, W. R., Schmidt-Base, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G. & Holden, H. M. (1993b). Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261(5117), 50-8.

Rayment, I., Smith, C. & Yount, R. G. (1996). The active site of myosin. [Review] [146 refs]. Annual Review of Physiology 58, 671-702.

Ritchie, M. D., Geeves, M. A., Woodward, S. K. & Manstein, D. J. (1993). Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum. Proceedings of the National Academy of Sciences of the United States of America 90(18), 8619-23.

Schroeder, R. R., Manstein, D. J., Jahn, W., Holden, H., Rayment, I., Holmes, K. C. & Spudich, J. A. (1993). Three-dimensional atomic model of F-actin decorated with Dictyostelium myosin S1. Nature 364(6433), 171-4.

Siemankowski, R. F. & White, H. D. (1984). Kinetics of the interaction between actin, ADP, and cardiac myosin-S1. Journal of Biological Chemistry 259(8), 5045-53.

Smith, C. A. & Rayment, I. (1996a). X-ray structure of the magnesium(ii) .adp.vanadate complex of the dictyostelium-discoideum myosin motor domain to 1.9Å resolution. Biochemistry 35(17), 5404-5417.

Smith, C. A. & Rayment, I. (1996b). Active site comparisons highlight structural similarities between myosin and other P-loop proteins. Biophys. J. 70, 1590-1602.

Taylor, E. W. (1991). Kinetic studies on the association and dissociation of myosin subfragment 1 and actin. Journal of Biological Chemistry 266(1), 294-302.

Trentham, D. R., Eccleston, J. F. & Bagshaw, C. R. (1976). Kinetic analysis of ATPase mechanisms. Quarterly Reviews of Biophysics 9(2), 217-81.

Uyeda, T. Q., Abramson, P. D. & Spudich, J. A. (1996). The neck region of the myosin motor domain acts as a lever arm to generate movement. Proceedings of the National Academy of Sciences of the United States of America 93(9), 4459-64.

VanBuren, P., Waller, G. S., Harris, D. E., Trybus, K. M., Warshaw, D. M. & Lowey, S. (1994). The essential light chain is required for full force production by skeletal muscle myosin. Proceedings of the National Academy of Sciences of the United States of America 91(26), 12403-7.

Walker, M., Zhang, X. Z., Jiang, W., Trinick, J. & White, H. D. (1999). Observation of transient disorder during myosin subfragment-1 binding to actin by stopped-flow fluorescence and millisecond time resolution electron cryomicroscopy: Evidence that the start of the crossbridge power stroke in muscle has variable geometry. Proceedings of the National Academy of Sciences of the United States of America 96(2), 465-470.

Waller, G. S., Ouyang, G., Swafford, J., Vibert, P. & Lowey, S. (1995). A minimal motor domain from chicken skeletal muscle myosin. Journal of Biological Chemistry 270(25), 15348-52.

Webb, M. R. & Trentham, D. R. (1981). The mechanism of ATP hydrolysis catalyzed by myosin and actomyosin, using rapid reaction techniques to study oxygen exchange. Journal of Biological Chemistry 256(21), 10910-6.

White, H. D. & Rayment, I. (1993). Kinetic characterization of reductively methylated myosin subfragment 1. Biochemistry 32(37), 9859-65.

White, H. D. & Taylor, E. W. (1976). Energetics and mechanism of actomyosin adenosine triphosphatase. Biochemistry 15(26), 5818-26.

Whittaker, M., Wilson-Kubalek, E. M., Smith, J. E., Faust, L., Milligan, R. A. & Sweeney, H. L. (1995). Smooth muscle myosin moves 35Å upon ADP release. Nature 378, 748-751.

Woodward, S. K., Eccleston, J. F. & Geeves, M. A. (1991). Kinetics of the interaction of 2'(3')-O-(N-methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1: characterization of two acto-S1-ADP complexes. Biochemistry 30(2), 422-30.

Xie, X., Harrison, D. H., Schlichting, I., Sweet, R. M., Kalabokis, V. N., Szent-Gyorgyi, A. G. & Cohen, C. (1994). Structure of the regulatory domain of scallop myosin at 2.8 A resolution. Nature 368(6469), 306-12.

Yount, R. G., Lawson, D. & Rayment, I. (1995). Is myosin a "back door" enzyme? Biophysical Journal 68(4 Suppl), 47S-49S.