Energetics of Biological Macromolecules, Part E focuses on methods related to allosteric enzymes and receptors, including fluorescent proves, spectroscopic methods and quantitative analysis as well as on cooperativity in protein folding. NMR and mass spectrometry methods are discussed.
Allosteric Enzymes and Receptors
Cooperativity in Protein Folding and Assembly
Energetics of Biological Macromolecules, Part E focuses on methods related to allosteric enzymes and receptors, including fluorescent proves, s...
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...
In the past several years, there has been an explosion in the ability of biologists, molecular biologists and biochemists to collect vast amounts of d...
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. 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...
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 im...