Energetics of Biological Macromolecules / Edition 1

Hardcover (Print)
Used and New from Other Sellers
Used and New from Other Sellers
from $8.29
Usually ships in 1-2 business days
(Save 88%)
Other sellers (Hardcover)
  • All (6) from $8.29   
  • New (1) from $91.14   
  • Used (5) from $0.00   
Sort by
Page 1 of 1
Showing All
Note: Marketplace items are not eligible for any BN.com coupons and promotions
Seller since 2010

Feedback rating:



New — never opened or used in original packaging.

Like New — packaging may have been opened. A "Like New" item is suitable to give as a gift.

Very Good — may have minor signs of wear on packaging but item works perfectly and has no damage.

Good — item is in good condition but packaging may have signs of shelf wear/aging or torn packaging. All specific defects should be noted in the Comments section associated with each item.

Acceptable — item is in working order but may show signs of wear such as scratches or torn packaging. All specific defects should be noted in the Comments section associated with each item.

Used — An item that has been opened and may show signs of wear. All specific defects should be noted in the Comments section associated with each item.

Refurbished — A used item that has been renewed or updated and verified to be in proper working condition. Not necessarily completed by the original manufacturer.

ETA - Standard Mail takes 6-10 business days & Expedited Mail takes 4-6 business days to deliver an item. We do not ship to APO-FPO addresses.

Ships from: Missouri City, TX

Usually ships in 1-2 business days

  • Standard, 48 States
  • Standard (AK, HI)
  • Express, 48 States
  • Express (AK, HI)
Page 1 of 1
Showing All
Sort by


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.

Read More Show Less

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."
"Incomparably useful."
"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."
"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."
"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."
"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."
"A series that has established itself as a definitive reference for biochemists."
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.
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
Read More Show Less

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.

Read More Show Less

Customer Reviews

Be the first to write a review
( 0 )
Rating Distribution

5 Star


4 Star


3 Star


2 Star


1 Star


Your Rating:

Your Name: Create a Pen Name or

Barnes & Noble.com Review Rules

Our reader reviews allow you to share your comments on titles you liked, or didn't, with others. By submitting an online review, you are representing to Barnes & Noble.com that all information contained in your review is original and accurate in all respects, and that the submission of such content by you and the posting of such content by Barnes & Noble.com does not and will not violate the rights of any third party. Please follow the rules below to help ensure that your review can be posted.

Reviews by Our Customers Under the Age of 13

We highly value and respect everyone's opinion concerning the titles we offer. However, we cannot allow persons under the age of 13 to have accounts at BN.com or to post customer reviews. Please see our Terms of Use for more details.

What to exclude from your review:

Please do not write about reviews, commentary, or information posted on the product page. If you see any errors in the information on the product page, please send us an email.

Reviews should not contain any of the following:

  • - HTML tags, profanity, obscenities, vulgarities, or comments that defame anyone
  • - Time-sensitive information such as tour dates, signings, lectures, etc.
  • - Single-word reviews. Other people will read your review to discover why you liked or didn't like the title. Be descriptive.
  • - Comments focusing on the author or that may ruin the ending for others
  • - Phone numbers, addresses, URLs
  • - Pricing and availability information or alternative ordering information
  • - Advertisements or commercial solicitation


  • - By submitting a review, you grant to Barnes & Noble.com and its sublicensees the royalty-free, perpetual, irrevocable right and license to use the review in accordance with the Barnes & Noble.com Terms of Use.
  • - Barnes & Noble.com reserves the right not to post any review -- particularly those that do not follow the terms and conditions of these Rules. Barnes & Noble.com also reserves the right to remove any review at any time without notice.
  • - See Terms of Use for other conditions and disclaimers.
Search for Products You'd Like to Recommend

Recommend other products that relate to your review. Just search for them below and share!

Create a Pen Name

Your Pen Name is your unique identity on BN.com. It will appear on the reviews you write and other website activities. Your Pen Name cannot be edited, changed or deleted once submitted.

Your Pen Name can be any combination of alphanumeric characters (plus - and _), and must be at least two characters long.

Continue Anonymously

    If you find inappropriate content, please report it to Barnes & Noble
    Why is this product inappropriate?
    Comments (optional)