This book consists of 11 chapters and begins with a brief overview of enzyme structure, followed by a discussion on methods of probing enzyme structure such as X-ray crystallography and optical spectroscopy. Kinetic methods are then described, with emphasis on the general principles of steady-state and transient kinetics. The chemical principles involved in enzyme catalysis are also discussed, and case studies of a few well-documented enzymes are presented. The regulation of enzyme activity is analyzed from a nongenetic viewpoint, with particular reference to binding isotherms and models for allosterism. Two particular enzymes, aspartate transcarbamoylase and phosphofructokinase, are used as examples of well-studied regulatory enzymes. The last two chapters focus on multienzyme complexes and membrane-bound enzymes.
This monograph is intended for graduate students, advanced undergraduates, and research workers in molecular biology and biochemistry.
This practical, up-to-date survey is designed for a broad spectrum of biological and chemical scientists who are beginning to delve into modern enzymology. Enzymes, Second Edition explains the structural complexities of proteins and enzymes and the mechanisms by which enzymes perform their catalytic functions. The book provides illustrative examples from the contemporary literature to guide the reader through concepts and data analysis procedures. Clear, well-written descriptions simplify the complex mathematical treatment of enzyme kinetic data, and numerous citations at the end of each chapter enable the reader to access the primary literature and more in-depth treatments of specific topics.
This Second Edition of Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis features refined and expanded coverage of many concepts, while retaining the introductory nature of the book. Important new features include:A new chapter on protein-ligand binding equilibria Expanded coverage of chemical mechanisms in enzyme catalysis and experimental measurements of enzyme activity Updated and refined discussions of enzyme inhibitors and multiple substrate reactions Coverage of current practical applications to the study of enzymology
Supplemented with appendices providing contact information for suppliers of reagents and equipment for enzyme studies, as well as a survey of useful Internet sites and computer software for enzymatic data analysis, Enzymes, Second Edition is the ultimate practical guide for scientists and students in biochemical, pharmaceutical, biotechnical, medicinal, and agricultural/food-related research.
Advances in such fields as proteomics and genomics place new demands on students and professionals to be able to apply quantitative concepts to the biological phenomena that they are studying. Spectroscopy for the Biological Sciences provides students and professionals with a working knowledge of the physical chemical aspects of spectroscopy, along with their applications to important biological problems.
Designed as a companion to Professor Hammes's Thermodynamics and Kinetics for the Biological Sciences, this approachable yet thorough text covers the basic principles of spectroscopy, including:
* Fundamentals of spectroscopy
* Electronic spectra
* Circular dichroism and optical rotary dispersion
* Vibration in macromolecules (IR, Raman, etc.)
* Magnetic resonance
* X-ray crystallography
* Mass spectrometry
With a minimum of mathematics and a strong focus on applications to biology, this book will prepare current and future professionals to better understand the quantitative interpretation of biological phenomena and to utilize these tools in their work.
Introduction to Macromolecular Binding Equilibria gives students in medicinal chemistry, pharmaceuticals, and bioengineering the necessary background in biophysical chemistry for research applications in drug discovery and development. Building upon a fundamental knowledge of calculus and physical chemistry, this compact, graduate-level text prepares students for advanced work in solution thermodynamics and binding phenomena and applying methods in this book to their own research.
This book describes the underlying theory of binding phenomena and explains how to apply the binding polynomial approach for building models and interpreting data. It also covers practical considerations for setting up binding experiments and describes how to obtain true thermodynamic isotherms unbiased by model assumption via model-free analysis of binding data.
With more than 350 color images throughout, Introduction to Proteins: Structure, Function, and Motion presents a unified, in-depth treatment of the relationship between the structure, dynamics, and function of proteins. Taking a structural–biophysical approach, the authors discuss the molecular interactions and thermodynamic changes that transpire in these highly complex molecules.
The text incorporates various biochemical, physical, functional, and medical aspects. It covers different levels of protein structure, current methods for structure determination, energetics of protein structure, protein folding and folded state dynamics, and the functions of intrinsically unstructured proteins. The authors also clarify the structure–function relationship of proteins by presenting the principles of protein action in the form of guidelines.
This comprehensive, color book uses numerous proteins as examples to illustrate the topics and principles and to show how proteins can be analyzed in multiple ways. It refers to many everyday applications of proteins and enzymes in medical disorders, drugs, toxins, chemical warfare, and animal behavior. Downloadable questions for each chapter are available at CRC Press Online.
This biennial conference, organized by APDIO, the Portuguese Association of Operational Research, held in Bragança, Portugal, in June 2013, presented a perfect opportunity to discuss the latest development in this field and to narrow the gap between academic researchers and practitioners.