By Monique M. Tirion, Daniel ben-Avraham, Kenneth C. Holmes (auth.), James E. Estes, Paul J. Higgins (eds.)
During the interval August 5-9, 1992, and instantly previous the 1992 Gordon study convention on Motile and Contractile structures, the "Third overseas convention at the constitution and serve as of Ubiquitous mobile Protein Actin" was once held on the Emma Willard college in Troy, big apple, less than the name "ACTIN '92". This convention interested by the elemental houses and mobile capabilities of actin and actin established microfilament structures. the 1st convention during this sequence used to be held in 1982, in Sydney, Australia, and hosted via Dr. Cristobal G. dos Remedios and Dr. Julian A. Barden, either from the college of Sydney (New South Wales, Austrailia). the second one convention convened in Monza, Italy in June 1987, and was once equipped through Dr. Roberto Colombo, college of Milan (Italy). This 3rd amassing of researchers dedicated to the learn of actin and actin-associated proteins used to be geared up via Dr. James E. Estes, Albany Stratton V A scientific middle and Dr. Paul 1. Higgins, Albany clinical university, who have been assisted by means of an Organizing Committee along with Dr. Edward D. Korn (National middle, Lung and Blood Institute, NIH), Dr. Thomas P. Stossel (Massachusetts normal Hospital), Dr. Fumio Matsumura (Rutgers University), and Dr. Stephen Farmer (Boston University). This assembly was once devoted to the various pioneering contributions of Professor Fumio Oosawa to the sphere of actin research.
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Additional info for Actin: Biophysics, Biochemistry, and Cell Biology
Sample text
1992). , 1989). The binding kinetics for Mg+ + are somewhat different. , 1987). This implies that kMg> the association rate constant for Mg+ +, must be smaller than kea, the association rate constant for Ca ++, by a factor of 50 or so. , 1991) showed that this is indeed the case. kea was measured to be 2 x 107 M-lsec-l which, allowing for the geometry of the binding site, probably reflects diffusion limited association. 5 x lOS M-lsec-l, much too small for diffusion limited association. The low values for kM and k_Mg reflect the slow kinetics of the Mg+ + aquo-ion.
13: 263. Kuroda, M. & Maruyama, K,1972, Polymorphism of F-actin. II. ATPase activity at acid pH, J. Biochem. 71:39-45. , 1962, Deoxy ATP (or GTP) do not bind to G-actin, Biochim. Biophys. Acta 57: 163. , 1992, Crystallization of actin in complex with actin-binding proteins, J. Bioi. Chem. 267:11661-11664. Mihashi, K, 1984, Ca2+-dependent regulation of the subunit exchange of F-actin under the influence of tropomyosin and troponin. J. Biochem. 96:273-276. D. , 1986, Fluorescence energy transfer between nucleotide binding sites in an F-actin filament, Biochim.
1982, Kinetic analysis of actin assembly suggests that tropomyosin inhibits spontaneous fragmentation of actin filaments,]. Mol. Bioi. 161:217-227 Yanagida, T. , 1980, Conformational changes of F-actin-e-ADP in thin filaments in myosinfree muscle fibres induced by calcium, J. Mol. Bioi. 140:313-320. S. , 1987, Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction, Ann. Rev. Biophys. Chem. 16:535-559. 34 ACTIN-BOUND NUCLEOTIDE/DIVALENT CATION INTERACTIONS Lewis C.