Biothermodynamics

by Ackers, Gary K. Holt, Jo M. Johnson, Michael L.

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Title Statements

Full title :Biothermodynamics. / edited by Michael L. Johnson, Jo M. Holt and Gary K. Ackers.

Summary

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

Edition Statements

Publication Date:©2011.

Publication Statements

Publisher(s):Elsevier/Academic Press
Place of Publication:Amsterdam, Netherlands
Language:eng
Publication Date:©2011.

The Physical Object

Description:1 online resource (xliii, 323 pages, 8 unnumbered pages of plates) : : illustrations (some color)

Edition Identifiers

ISBN:9780123860040, 0123860040, 9780123860033, 0123860032
oclc:ocn742396471
LC Classification:QP601
Dewey Decimal:574.1925

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.

Subjects

Carrier Proteins Interactions protéine-protéine Ligands Ligands (Biochemistry) Ligands (Biochimie) Protein Array Analysis Protein Binding Protein-protein interactions Protéines -- Fixation Protéines de liaison SCIENCE -- Life Sciences thermodynamics Thermodynamique