Biothermodynamics. Part D [electronic resource] / edited by Michael L. Johnson, Jo M. Holt and Gary K. Ackers.

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.

Description based on 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.