Biothermodynamics. Part D / edited by Michael L. Johnson, Jo M. Holt and Gary K. Ackers.Material type: TextSeries: Methods in enzymology ; v. 492.Publication details: Amsterdam, Netherlands ; Boston, Mass. : Elsevier/Academic Press, ©2011. Description: 1 online resource (xliii, 323 pages, 8 unnumbered pages of plates) : illustrations (some color)Content type: text Media type: computer Carrier type: online resourceISBN: 9780123860040; 0123860040; 9780123860033; 0123860032Subject(s): Thermodynamics | Protein binding | Protein-protein interactions | Ligands (Biochemistry) | Ligands | Protein Array Analysis | Carrier Proteins | Thermodynamics | SCIENCE -- Life Sciences -- Biochemistry | Ligands (Biochemistry) | Protein binding | Protein-protein interactions | ThermodynamicsGenre/Form: Electronic books. | Electronic books. Additional physical formats: Print version:: Biothermodynamics. Part D.DDC classification: 574.1925 LOC classification: QP601 | .M49eb v. 492Online resources: Click here to access online
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Includes bibliographical references and indexes.
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.
Print version record.
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