Biothermodynamics, Part C
Series: Methods in Enzymology; 488;
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Product details:
- Publisher Elsevier Science
- Date of Publication 22 February 2011
- ISBN 9780123812681
- Binding Hardback
- No. of pages401 pages
- Size 228x152 mm
- Weight 790 g
- Language English 0
Categories
Long description:
"
In the past several years, there has been an explosion in the ability of biologists, molecular biologists and biochemists to collect vast amounts of data on their systems. Biothermodynamics, Part C presents sophisticated methods for estimating the thermodynamic parameters of specific protein-protein, protein-DNA and small molecule interactions.
The use of thermodynamics in biological research is used as an ""energy book-keeping system.ï¿1⁄2 While the structure and function of a molecule is important, it is equally important to know what drives the energy force. These methods look to answer: What are the sources of energy that drive the function? Which of the pathways are of biological significance?
As the base of macromolecular structures continues to expand through powerful techniques of molecular biology, such as X-ray crystal data and spectroscopy methods, the importance of tested and reliable methods for answering these questions will continue to expand as well.
" MoreTable of Contents:
- Measurement and Analysis of Equilibrium Binding Titrations: A beginner's guide
- Macromolecular Competition Titration Method: Accessing Thermodynamics of the Unmodified Macromolecule - Ligand Interactions Through Spectroscopic Titrations of Fluorescent Analogs
- Analysis of PKR-RNA interactions by sedimentation velocity
- Structural and Thermodynamic Analysis of PDZ/Ligand Interactions
- Thermodynamic analysis of metal ion-induced protein assembly
- Thermodynamic Dissection of Colicin Interactions
- Energetics of Src homology domain interactions in receptor tyrosine kinase-mediated signaling
- Structural and Functional Energetic Linkages in Allosteric Regulation of Muscle Pyruvate Kinase
- Analysis of Free Energy versus Temperature Curves in Protein Folding and Macromolecular Interactions
- Application of the Sequential n-Step Kinetic Mechanism to Polypeptide Translocases
- A Coupled Equilibrium Approach to Study Nucleosome Thermodynamics
- Quantitative methods for measuring DNA flexibility in vitro and in vivo
- 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 co-solutes
- Small Angle X-ray Scattering Studies of Peptide-Lipid Interactions using the Mouse Paneth Cell ?-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
Dorothy Beckett
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