Energetics of Biological Macromolecules, Part D: Volume 379
Published on 2. April 2004
Book
Hardback
281 pages
978-0-12-182783-0 (ISBN)
Description
This volume focuses on the cooperative binding aspects of energetics in biological macromolecules. Methodologies such as NMR, small-angle scattering techniques for analysis, calorimetric analysis, fluorescence quenching, and time resolved FRET measurements are discussed.
Reviews / Votes
"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection."CHEMISTRY IN INDUSTRY
More details
Series
Language
English
Place of publication
San Diego
United States
Publishing group
Elsevier Science Publishing Co Inc
Target group
Professional and scholarly
Biochemists, biophysicists, bioengineers, molecular biologists, structural biologists
Illustrations
Approx. 100 illustrations
Dimensions
Height: 229 mm
Width: 152 mm
Weight
570 gr
ISBN-13
978-0-12-182783-0 (9780121827830)
Copyright in bibliographic data and cover images is held by Nielsen Book Services Limited or by the publishers or by their respective licensors: all rights reserved.
Schweitzer Classification
Other editions
Additional editions
Michael Johnson | Jo M. Holt | Michael L. Johnson
Energetics of Biological Macromolecules, Part D
E-Book
05/2014
Academic Press
€155.00
Available for download
Persons
Edited by Michael L. Johnson, Gary K. Ackers and Jo M. Holt
Content
Analyzing Intermediate State Cooperativity in Hemoglobin; Nuclear Magnetic Resonance Spectroscopy in the Study of Hemoglobin Cooperativity; Evaluating Cooperativity in Dimeric Hemoglobins; Measuing Assembly and Binding in Human Embryonic Hemoglobins; Small-Angle Scattering Techniques for Analyzing; Conformational Transitions in Hemocyanins; Multivalent Protein-Carbohydrate Interactions: Isothermal Titration Microcalorimetry Studies; Calorimetric Analysis of Mutagenic Effects on Protein-Ligand Interactions; Multiple Binding of Ligands to a Linear Biopolymer; Probing Site-Specific Energetics in Proteins and Nucleic Acids by Hydrogen Exchange and Nuclear Magnetic Resonance Spectroscopy; Fluorescence Quenching Methods to Study Protein-Nucleic Acid interactions; Thermodynamics, Protein Modification, and Molecular Dynamics in Characterizing Lactose Repressor Protein: Strategies for Complex Analyses of Protein Structure-Function; Linked Equilibria in Biotin Repressor Function: Thermodynamics, Structural, and Kinetic Analysis; Distance Parameters Derived from Time-Resolved Foerster Resonance Energy Transfer Measurements and Their Use in Structural Interpretations of Thermodynamic Quantities Associated with Protein-DNA Interactions