[Methods in Enzymology] Biothermodynamics, Part A Volume 455 || Chapter 10 Characterization of Parvalbumin and Polcalcin Divalent Ion Binding by Isothermal Titration Calorimetry

✍ Scribed by Henzl, Michael T.

• Book ID: 121652565
• Publisher: Elsevier
• Year: 2009
• Tongue: English
• Weight: 829 KB
• Edition: 1
• Category: Article
• ISBN: 0123745969
• ISSN: 0076-6879
• DOI: 10.1016/S0076-6879(08)04210-9

✦ Synopsis

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. This volume 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.