Biothermodynamics, Part C | Buch | 978-0-12-381268-1 | sack.de

Buch, Englisch, 401 Seiten, Format (B × H): 152 mm x 229 mm, Gewicht: 790 g

Biothermodynamics, Part C


Erscheinungsjahr 2011
ISBN: 978-0-12-381268-1
Verlag: William Andrew Publishing

Buch, Englisch, 401 Seiten, Format (B × H): 152 mm x 229 mm, Gewicht: 790 g

ISBN: 978-0-12-381268-1
Verlag: William Andrew Publishing


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.� 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.
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Zielgruppe


Researchers in academics and industry studying biochemistry.

Weitere Infos & Material


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- Analysis of PKR-RNA interactions by sedimentation velocity

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- Structural and Thermodynamic Analysis of PDZ/Ligand Interactions

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- Thermodynamic Dissection of Colicin Interactions

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- Energetics of Src homology domain interactions in receptor tyrosine kinase-mediated signaling

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- Structural and Functional Energetic Linkages in Allosteric Regulation of Muscle Pyruvate Kinase

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- Analysis of Free Energy versus Temperature Curves in Protein Folding and Macromolecular Interactions

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- A Thermodynamic Approach for the Targeting of Nucleic Acid Structures Using Their Complementary Single Strands

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- Protein stability in the presence of co-solutes

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- Small Angle X-ray Scattering Studies of Peptide-Lipid Interactions using the Mouse Paneth Cell a-Defensin Cryptdin-4

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- Non-B Conformations of CAG Repeats Using 2-aminopurine

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- 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

Travis P. Schrank, W. Austin Elam, Jing Li and Vincent J. Hilser


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