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Biothermodynamics. Part D /

The use of thermodynamics in biological research can be equated to an energy book-keeping system. While the structure and function of a molecule is important, it is equally important to know what drives the energy force. This volume presents sophisticated methods for estimating the thermodynamic par...

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Johnson, Michael L., 1947-, Holt, Jo M., Ackers, Gary K.
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Amsterdam, Netherlands ; Boston, Mass. : Elsevier/Academic Press, �2011.
Colección:Methods in enzymology ; v. 492.
Temas:
Acceso en línea:Texto completo
Texto completo
Texto completo

MARC

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245 0 0 |a Biothermodynamics.  |n Part D /  |c edited by Michael L. Johnson, Jo M. Holt and Gary K. Ackers. 
260 |a Amsterdam, Netherlands ;  |a Boston, Mass. :  |b Elsevier/Academic Press,  |c �2011. 
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490 1 |a Methods in enzymology,  |x 0076-6879 ;  |v v. 492 
504 |a Includes bibliographical references and indexes. 
505 0 |a A thermodynamic approach for the targeting of nucleic acid structures using their complementary single strands -- Thermodynamics of biological processes -- Protein stability in the presence of cosolutes -- Small-angle X-ray scattering studies of peptide-lipid interactions using the mouse paneth cell [alpha]-defensin cryptdin-4 -- Synergy of molecular dynamics and isothermal titration calorimetry in studies of allostery -- Using tryptophan fluorescence to measure the stability of membrane proteins folded in liposomes -- Non-B conformations of CAG repeats using 2-aminopurine -- Disulfide bond-mediated passenger domain stalling as a structural probe of autotransporter outer membrane secretion in vivo -- Strategies for the thermodynamic characterization of linked binding/local folding reactions within the native state application to the lid domain of adenylate kinase from Escherichia coli -- Fluorescence-detected sedimentation in dilute and highly concentrated solutions. 
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520 |a The use of thermodynamics in biological research can be equated to an energy book-keeping system. While the structure and function of a molecule is important, it is equally important to know what drives the energy force. This volume presents sophisticated methods for estimating the thermodynamic parameters of specific protein-protein, protein-DNA and small molecule interactions. * Elucidates the relationships between structure and energetics and their applications to molecular design, aiding researchers in the design of medically important molecules * Provides a "must-have" methods volume that keeps MIE buyers and online subscribers up-to-date with the latest research * Offers step-by-step lab instructions, including necessary equipment, from a global research community 
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