Binding and Linkage

Binding and Linkage PDF

Author: Jeffries Wyman

Publisher: University Science Books

Published: 1990

Total Pages: 358

ISBN-13: 9780935702569

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Ligand-macromolecule interactions are of fundamental importance in the control of biological processes. This book applies the principles of linkage thermodynamics to polyfunctional macromolecular systems under equilibrium conditions, and describes the binding, linkage, and feedback phenomena that lead to control of complex metabolic processes. The first chapter sets out the different processes (conformational changes, changes in state of aggregation, phase changes) involving biological macromolecules which are affected by chemical variables (such as ligands) or physical variables (such as temperature and pressure). The general effects of ligands on micromolecular conformations and interactions are illustrated with specific examples from the respiratory proteins, electron-transport proteins, and nucleic acid binding proteins. Subsequent chapters develop these themes, and describe in detail how the mathematics of regulation and control can be applied to macromolecules in biological system.

Studyguide for Binding and Linkage

Studyguide for Binding and Linkage PDF

Author: Cram101 Textbook Reviews

Publisher: Cram101

Published: 2014-05-28

Total Pages: 66

ISBN-13: 9781490298283

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Never HIGHLIGHT a Book Again! Includes all testable terms, concepts, persons, places, and events. Cram101 Just the FACTS101 studyguides gives all of the outlines, highlights, and quizzes for your textbook with optional online comprehensive practice tests. Only Cram101 is Textbook Specific. Accompanies: 9781891389641. This item is printed on demand.

Linkage Thermodynamics of Macromolecular Interactions

Linkage Thermodynamics of Macromolecular Interactions PDF

Author:

Publisher: Academic Press

Published: 1998-06-24

Total Pages: 485

ISBN-13: 0080582249

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This volume commemorates the 50th anniversary of the appearance in Volume 4 in 1948 of Dr. Jeffries Wyman's famous paper in which he "laid down" the foundations of linkage thermodynamics. Experts in this area contribute articles on the state-of-the-art of this important field and on new developments of the original theory. Among the topics covered in this volume are electrostatic contributions to molecular free energies in solution; site-specific analysis of mutational effects in proteins; allosteric transitions of the acetylcholine receptor; and deciphering the molecular code of hemoglobin allostery.

Energetics of Biological Macromolecules

Energetics of Biological Macromolecules PDF

Author: Michael L. Johnson

Publisher: Elsevier

Published: 1998

Total Pages: 596

ISBN-13: 9780121821968

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Essential publication for researchers in all fields of life sciences. Key Features * Major topics covered include: * Deciphering rules of helix stability in peptides * Protein Folding in Membranes * Molecular Crowding * Study of the Bohr Effect in Hemoglobin Intermediates * Photoacoustic Calorimetry of Proteins * Theoretical Aspects of Isothermal Titration Calorimetry * Energetic Methods to Study Bifunctional Biotin Repressor.

Protein–Ligand Binding Thermodynamics

Protein–Ligand Binding Thermodynamics PDF

Author: Justin M. Miller

Publisher: American Chemical Society

Published: 2023-06-01

Total Pages: 217

ISBN-13: 084129979X

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Ligand binding by macromolecules represents a core event of broad relevance to a range of systems, including catalytic systems alongside noncatalytic systems such as nucleic acid binding by transcription factors or extracellular ligand binding by proteins involved in signaling pathways. The scope of this primer is constrained to introduce only foundational models without significant discussion of more advanced topics such as allosteric or linkage effects. Linkage occurs when the binding of a ligand is influenced by the binding of another molecule of the same ligand (homotropic linkage), the binding of a different ligand (heterotropic linkage), physical variables such as temperature or pressure (physical linkage), or changes in macromolecular assembly state (polysteric linkage). Taking this into account, the foundational themes presented in this primer can be used to describe any macromolecule–ligand interaction either by direct use of the models and techniques described here or by applying them to develop more advanced models to explain additional complexities such as those allosteric or linkage effects just mentioned. The target audience of this primer is the senior undergraduate or junior graduate student who lacks a foundation in ligand-binding thermodynamics. As such, we have focused primarily on foundational thermodynamic treatments and presented only general discussions of relevant experimental designs. Readers of this primer will learn how to build a working understanding of common factors that promote energetic favorability for ligand binding; develop a functional toolbox to understand ligand binding from the perspective of collecting, plotting, and interpreting ligand-binding data; enhance proficiency in deriving thermodynamic mechanisms for ligand binding; and become comfortable in interpreting binding data reported in the literature and independently expanding knowledge beyond the scope introduced in this primer.

Introduction to Macromolecular Binding Equilibria

Introduction to Macromolecular Binding Equilibria PDF

Author: Charles P. Woodbury

Publisher: CRC Press

Published: 2007-11-08

Total Pages: 272

ISBN-13: 1420052993

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Macromolecules in the body form noncovalent associations, such as DNA-protein or protein-protein complexes, that control and regulate numerous cellular functions. Understanding how changes in the concentration and conformation of these macromolecules can trigger physiological responses is essential for researchers developing drug therapies to treat

Reversible Ligand Binding

Reversible Ligand Binding PDF

Author: Andrea Bellelli

Publisher: John Wiley & Sons

Published: 2018-01-09

Total Pages: 309

ISBN-13: 111923848X

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Presents the physical background of ligand binding and instructs on how experiments should be designed and analyzed Reversible Ligand Binding: Theory and Experiment discusses the physical background of protein-ligand interactions—providing a comprehensive view of the various biochemical considerations that govern reversible, as well as irreversible, ligand binding. Special consideration is devoted to enzymology, a field usually treated separately from ligand binding, but actually governed by identical thermodynamic relationships. Attention is given to the design of the experiment, which aids in showing clear evidence of biochemical features that may otherwise escape notice. Classical experiments are reviewed in order to further highlight the importance of the design of the experiment. Overall, the book supplies students with the understanding that is necessary for interpreting ligand binding experiments, formulating plausible reaction schemes, and analyzing the data according to the chosen model(s). Topics covered include: theory of ligand binding to monomeric proteins; practical considerations and commonly encountered problems; oligomeric proteins with multiple binding sites; ligand binding kinetics; hemoglobin and its ligands; single-substrate enzymes and their inhibitors; two-substrate enzymes and their inhibitors; and rapid kinetic methods for studying enzyme reactions. Bridges theory of ligand binding and allostery with experiments Applies historical and physical insight to provide a clear understanding of ligand binding Written by a renowned author with long-standing research and teaching expertise in the area of ligand binding and allostery Based on FEBS Advanced Course lectures on the topic Reversible Ligand Binding: Theory and Experiment is an ideal text reference for students and scientists involved in biophysical chemistry, physical biochemistry, biophysics, molecular biology, protein engineering, drug design, pharmacology, physiology, biotechnology, and bioengineering.

The Amide Linkage

The Amide Linkage PDF

Author: Arthur Greenberg

Publisher: John Wiley & Sons

Published: 2002-11-11

Total Pages: 672

ISBN-13: 9780471420255

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An authoritative reference to an important and ubiquitous chemical linkage The amide linkage is one of the most fundamental and widespread chemical bonds in nature, underlying the properties of a vast array of organic molecules, polymers, and materials, including peptides and proteins. Arthur Greenberg, Curt Breneman, and Joel Liebman's peerless text provides comprehensive coverage of the experimental, structural, and computational findings that shed light on the chemical and physical properties of the amide linkage, as well as its emerging applications in materials and biotechnology. Chapters in The Amide Linkage highlight how this chemical bond factors in the design of enzyme inhibitors, cyclic peptides, antibacterial agents, and emerging nanotechnology applications. This one-of-a-kind study also: * Discusses selected aspects of chemical reactions, structure, bonding, and energetics of the amide bond, including amide rotational barriers, stereochemistry, complexation, spectroscopy, and thermochemistry * Presents specific applications to supramolecular and stereospecific synthesis * Discusses key aspects of peptide and protein chemistry-such as molecular recognition, conformation, and folding-in terms of the amide linkage * Includes chapters contributed by numerous eminent chemists and biochemists Organic, medicinal, polymer, and physical chemists, as well as biochemists and materials scientists, will find The Amide Linkage to be an invaluable addition to their professional libraries.