Energetics of Biological Macromolecules / Edition 1

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Overview

The critically acclaimed laboratory standard for forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerlyawaited, frequently consulted, and praised by researchers and reviewers alike. More than 250 volumes have been published (all of them still in print) and much of the material is relevant even today—truly an essential publication for researchers in all fields of life sciences.

Key Features
• Thermodynamics as a tool for understanding molecular logic
• Thermal denaturation methods in the study of protein folding
• Predicting thermodynamic properties of RNA
• Sedimentation equilibrium as a thermodynamic tool
• Molecular volume
• Thermodynamic parameters from hydrogen exchange measurements

Audience: Biochemists, biophysicists, molecular biologists, analytical chemists, and physiologists.

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Editorial Reviews

Doody's Review Service
Reviewer: Gene A. Homandberg, PhD (Rush Medical College of Rush University)
Description: This monograph in the Methods in Enzymology series presents contributions from 60 experts on thermodynamic methods for determining functional energetics of ligand interaction with macromolecules, conformational changes in protein and nucleic acids, macromolecular assembly, allosteric regulation, phase transitions, protein nucleic acid recognition, and the role and coupling of these processes in enzyme catalysis and other activities of macromolecules.
Purpose: The purpose is to review applications of various classical and newer methods used to study the energetics of biological macromolecules in many diverse systems. Additional overview or summary chapters that educate the reader on the importance of such studies or how such approaches can be linked together to describe a particular biologic system would have been helpful for less informed readers. Nonetheless, the chapters on studies of nucleic acid conformation and energetics of interaction with chemically modified DNA binding proteins will be particularly appealing to many molecular biologists and do illustrate the usefulness and currency of the described methods.
Audience: The book is intended for biochemists and molecular biologists in general. These topics should be particularly useful to many different types of researchers, including protein chemists, molecular biologists, enzymologists, and pharmaceutical biochemists.
Features: The monograph features informative black-and-white illustrations, all presented in an attractive format typical of this series and suitable in number, quality, and information content.
Assessment: This book should be very useful to researchers as well as students who study either protein or nucleic acids. Because some of the basic classical topics that have been covered before in other series are now brought more up to date and because the book illustrates current relevance by including studies of protein-nucleic acid interaction, this volume is more appealing to both students and experienced researchers studying biologic systems.
From the Publisher
Praise for the Series
"The Methods in Enzymology series represents the gold-standard."
—NEUROSCIENCE
"Incomparably useful."
—ANALYTICAL BIOCHEMISTRY
"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page."
—BIO/TECHNOLOGY
"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
"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced."
—AMERICAN SOCIETY OF MICROBIOLOGY NEWS
"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work."
—ENZYMOLOGIA
"A series that has established itself as a definitive reference for biochemists."
—JOURNAL OF CHROMATOGRAPHY
Gene A. Homandberg
This volume honors K.E. van Holde for his many contributions to studies of energetics of protein folding, protein assembly and biologic recognition, and ligand-ligand interaction. It includes 24 chapters by experts who cover areas including determination of the energetics of protein-bilayer interactions; molecular design of peptide ligands; study of the Bohr effect in hemoglobin interactions; and photoacoustic calorimetry of proteins and studies of interactions and folding of repressor proteins. This volume is meant to cover topics to which van Holde made contributions and to include newer methologic approaches and applications that should be of general interest. While some of these chapters are very specific, they illustrate the potential of these applications to other study systems. Nonetheless, this volume was not meant to be a general volume that focuses on only the most commonly used methods. The audience could include anyone from student to experienced structural biologist or protein chemist. Each chapter is well written, very concise, yet very informative, and should be interesting reading for investigators at different levels of training. This book should be informative to anyone with a need to understand how to characterize protein structure and activities and an interest in the specific methods and applications presented. The features include many informative illustrations with very useful, very extensive bibliographies. The book is in the form of the attractive Methods in Enzymology series. This would be a worthwhile addition to the library of anyone with interests in energetics of protein folding and protein ligand interaction. Since the editorsand contributors are internationally recognized experts, the content is very meaningful.
Booknews
The second ensemble in the series of biothermodynamic articles, especially useful for researchers and students whose goal is to connect the functional energetics of macromolecular structures with their biological functions. Twenty-four articles include tight ligand binding affinities determined from thermodynamic linkage to temperature by titration calorimetry; application of automated methods for determination of protein conformational stability; kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors; and energetic methods to study the bifunctional biotin operon repressor. Annotation c. by Book News, Inc., Portland, Or.

4 Stars! from Doody
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Product Details

  • ISBN-13: 9780121821609
  • Publisher: Elsevier Science
  • Publication date: 9/25/1995
  • Series: Methods in Enzymology Series
  • Edition description: New Edition
  • Edition number: 1
  • Pages: 761

Table of Contents

J.M. Holt and G.K. Ackers, Pathway of Allosteric Control as Revealed by Intermediate States of Hemoglobin.
Y. Huang and D.W. Bolen, Probes of Energy Transduction in Enzyme Catalysis.
V.A. Parsegian, R.P. Rand, and D.C. Rau, Macromolecules and Water: Probing with Osmotic Stress.
I. Wong and T.M. Lohman, Linkage of Protein Assembly to Protein-DNA Binding.
E. Di Cera, Q.D. Dang, Y. Ayala, and A. Vindigni, Linkage at Steady State: Allosteric Transitions of Thrombin.
E. Freire, Thermal Denaturation Methods in Study of Protein Folding.
L. Chen, R.L. Biltonen, and M.L. Johnson, Kinetics of Lipid Membrane Phase Transitions: A Volume Perturbation Calorimeter Study.
M.L. Doyle, G. Louie, P. Dal Monte, and T. Sokoloski, Tight Binding Affinities Determined from the Thermodynamic Linkage to Protons by Titration Calorimetry.
H.F. Fisher and N. Singh, Calorimetric Methods for Interpreting Protein-Ligand Interactions.
K.J. Breslauer, Extracting Thermodynamic Data from Equilibrium Melting Curves for Oligonucleotide Order-Disorder Transitions.
M.J. Serra and D.H. Turner, Predicting Thermodynamic Properties of RNA.
K.B. Hall and J.K. Kranz, Thermodynamics and Mutations in RNA-Protein Interactions.
D.E. Draper and T.C. Gluick, Melting Studies of RNA Unfolding and RNA-Ligand Interactions.
L. Jen-Jacobson, Structural-Perturbation Approaches to Thermodynamics of Site-Specific Protein-DNAInteractions.
Y. Bai, J.J. Englander, L. Mayne, J.S. Milne, and S.W. Englander, Thermodynamic Parameters from Hydrogen Exchange Measurements.
C.A. Royer, Application of Pressure to Biochemical Equilibria: The Other Thermodynamic Variable.
L.M. Rellick and W.J. Becktel, Molecular Volume.
C.R. Robinson and S.G. Sligar, Hydrostatic and Osmotic Pressure as Tools to Study Macromolecular Recognition.
T.M. Laue, Sedimentation Equilibrium as Thermodynamic Tool.
J. Yang and J. Carey, Footprint Phenotypes: Structural Models of DNA-Binding Proteins from Chemical Modification Analysis of DNA.
M. Perrella and I. Denisov, Low-Temperature Electrophoresis Methods.
M.R. Eftink, Use of Multiple Spectroscopic Methods to Monitor Equilibrium Unfolding of Proteins.
B. Garcia-Moreno, Probing Structural and Physical Basis of Protein Energetics Linked to Protons and Salt.
C.N. Pace, Evaluating Contribution of Hydrogen Bonding and Hydrophobic Bonding to Protein Folding.
B. Lee, Analyzing Solvent Reorganization and Hydrophobicity.
T.P. Creamer and G.D. Rose, Simple Force Field for Study of Peptide and Protein Conformational Properties.
M. Martinez-Carrion, A. Artigues, A. Berezov, M.L. Bianconi, A.M. Reyes, and A. Iriarte, Probes for Analysis of Stability of Different Variants of Aspartate Aminotransferase.
N.M. Allewell and V.J. LiCata, Thermodynamic Approaches to Understanding Aspartate Transcarbamylase.
R. Lumry, On the Interpretation of Data from Isothermal Processes.
Author Index.
Subject Index.

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