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By Monique M. Tirion, Daniel ben-Avraham, Kenneth C. Holmes (auth.), James E. Estes, Paul J. Higgins (eds.)

ISBN-10: 1461361028

ISBN-13: 9781461361022

ISBN-10: 1461525780

ISBN-13: 9781461525783

During the interval August 5-9, 1992, and instantly previous the 1992 Gordon study convention on Motile and Contractile structures, the "Third foreign convention at the constitution and serve as of Ubiquitous mobile Protein Actin" used to be held on the Emma Willard university in Troy, long island, below the name "ACTIN '92". This convention thinking about the elemental houses and mobile capabilities of actin and actin­ dependent microfilament structures. the 1st convention during this sequence was once 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 used to be equipped via 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 by way of Dr. James E. Estes, Albany Stratton V A scientific heart and Dr. Paul 1. Higgins, Albany clinical collage, who have been assisted via an Organizing Committee including Dr. Edward D. Korn (National center, 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 used to be devoted to the various pioneering contributions of Professor Fumio Oosawa to the sector of actin research.

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Extra resources for Actin: Biophysics, Biochemistry, and Cell Biology

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I. Bioi. Chem. 255:8991-8993. Frieden, C. 1982. The Mg-induced Conformational Change in Rabbit Skeletal Muscle G-actin. 1. Bioi. Chem. 257:2882-2886. Frieden, C. and K. Patane. 1988. Mechanism for Nucleotide Exchange in Monomeric Actin. Bio chemistry 27:3812-3820. , LA. E. Estes. 1986. High Affmity Binding of Divalent Cation to Actin Monomer is Much Stronger than Previously Reported. Biochem. Biophys. Res. Comm. 135:607-614. , LA. J. E. Estes. 1989. Preparation and polymerization properties of monomeric ADP-Actin.

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.

Thus the conversion of Ca-actin to Mg-actin generally requires the use of chelators and prolonged (5-10 min) exchange times. Lastly, it is prudent to check that the exchange to Mg-actin really is complete by determining the actinbound cation. 42 NUCLEOTIDE BINDING TO ACTIN Background Each actin molecule binds tightly one nucleotide, which is ATP or ADP under physiological conditions. , 1993, for review). The atomic structure of the actin:DNase I complex recently reported by Kabsch et al. (1990) makes clear the intimate relationship between the tightly bound divalent cation and nucleotide.

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Actin: Biophysics, Biochemistry, and Cell Biology by Monique M. Tirion, Daniel ben-Avraham, Kenneth C. Holmes (auth.), James E. Estes, Paul J. Higgins (eds.)


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