Biothermodynamics. Part D /

• Άλλοι συγγραφείς: Johnson, Michael L., 1947-, Holt, Jo M., Ackers, Gary K.
• Μορφή: Ηλ. βιβλίο
• Γλώσσα: English
• Έκδοση: Amsterdam, Netherlands ; Boston, Mass. : Elsevier/Academic Press, ©2011.
• Σειρά: Methods in enzymology ; v. 492.
• Θέματα: Thermodynamics.; Protein binding.; Protein-protein interactions.; Ligands (Biochemistry); SCIENCE > Life Sciences > Biochemistry.; Protein Binding.; Protein Array Analysis.; Ligands.; Electronic books.

 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. 

 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.