Multiple Equilibria in Proteins
1st Edition
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Description
Multiple Equilibria in Proteins covers the multiple interactions between small ions and molecules and a protein molecule. The book also deals with the physicochemical mechanisms of this interaction and the information about protein structure and the forces stabilizing that structure. The text discusses the mathematical description of complex formation, the thermodynamic analysis of binding data, and various theoretical models which can be used to describe the phenomena of small molecule-macromolecule interactions. The measurement of complex formation; the binding of neutral molecules; and hydrogen-ion equilibria are also considered. The book further tackles metal-ion binding; the binding of organic ions by proteins; as well as protein-protein interaction. Chemists and biochemists will find the book useful.
Table of Contents
Preface
I. Introduction
References
II. Thermodynamics and Model Systems
I. Introduction
II. Some Concepts in Thermodynamics
III. Multiple Binding without Interaction between Sites
IV. Binding with Interaction between Sites
A. Debye-Hückel-Born Treatment of Electrostatic Interaction
B. Tanford-Kirkwood Model for Electrostatic Interaction
C. Hill Model for Cylindrical Rods
V. Method of Data Treatment
VI. Thermodynamics of Multiple Equilibria
VII. Binding-Induced Phase Transitions
VIII. Linked Functions
References
III. The Measurement of Complex Formation
I. Introduction
II. Subtractive Methods
A. EMF Measurements of Free Ligand Activity
B. Equilibrium Dialysis
C. Ultrafiltration and Ultracentrifugation
D. Gel Filtration
E. Partition Equilibrium between Phases
F. Electrical Conductivity
G. Polarography
H. Determination of Free Ligand without Separation of Phases
III. Direct Measurements
A. Changes in Light Absorption of Ligand
B. Fluorescence Methods
C. Optical Rotation
D. Nuclear Magnetic Resonance
E. X-Ray Diffraction
F. Refractive Index
G. Light-Scattering and Osmotic Pressure
H. Biological Activity
IV. Electrostatic Methods
A. Electrophoresis
B. Changes in the Titration Curves of Proteins due to the Presence of Bound Ions
C. The pH Method of Scatchard and Black—Displacement of pH of Isoionic Solutions by Added Salt
D. Dielectric Increment and Dispersion
V. Other Methods
A. Complement Fixation
B. Methods which Depend on Competition
References
IV. Binding of Neutral Molecules
I. Introduction
II. Results Obtained with Particular Proteins
A. Serum Albumins
B. β-Lactoglobulin
C. Myoglobin and Hemoglobin
D. Lysozyme
E. Other Enzymes
F. Globulins
G. α-Acid Glycoprotein (Human)
H. Concanavalin A
I. Myosin
III. The Hydration of Proteins
A. The State of Combined Water
IV. Interactions with Other Solvents
A. Dependence on High Powers of Concentration
V. Mechanism of Binding of Neutral Molecules
References
V. Hydrogen-Ion Equilibria
I. Introduction
II. Prototropic Groups in Proteins
III. Some Experimental Details
A. Isoionic Point
B. Definition of pH
IV. An Experimental Titration Curve
V. Anomalies Illustrated by Specific Proteins
A. Bovine Serum Albumin—Abnormal Carboxylate Groups
B. ß-Lactoglobulin—Abnormal Carboxyl and Thiol Groups
C. Ribonuclease—Abnormal Phenolic Groups
D. Hemoglobin—Abnormal Imidazole Groups
E. Insulin and Zinc Insulin
F. Paramyosin, a Rodlike Protein
VI. Hydrogen-Ion Equilibria of Denatured Proteins
VII. Unfolding as a Function of Protonation
A. Bovine Serum Albumin
B. E. coli Alkaline Phosphatase
VIII. Summary
References
VI. Metal-Ion Binding
I. Metal Ions and Their Complexes in Solution
II. Experimental Methods and Data Treatment
III. Proteins Containing Metal Ions Necessary for Biological Activity
IV. Protein-Metal Complex Formation
A. Bovine Serum Albumin
B. Sperm Whale Myoglobin
C. Ribonuclease
D. Vasopressin and Oxytocin
E. Insulin
F. Membranes
G. Ribosomes
H. S-100, a Protein of the Nervous System
References
VII. Binding of Organic Ions by Proteins
I. Introduction
II. Large Organic Ions—Ionic Detergents
A. Early Work on Detergent Anions
B. Isotherms of Anionic Detergents
C. The Binding of Fatty Acids Compared to Other Ligands. Nature of the Binding Site
D. Criteria of Unfolding. Viscosity Deuterium Exchange, ORD, and Difference Spectra
E. Effects of pH on Anion Binding
F. Other Effects of Detergents on Proteins
G. Enthalpy Change in Binding. Uniqueness of Two Highest Energy Sites of BSA
H. Binding of Polyions
III. Dyes, Dye-Like, and Other Cyclic Molecules Binding as Ions
A. Early Work
B. The Affinities of Some Dyes to Proteins
C. Fluorescent Ligands
D. Dye Interactions with Denatured Protein
E. Protection by Dyes against Denaturation
F. Phytic Acid
IV. Binding of Small Nonaromatic Ions to Proteins
A. Early Work
B. Thermodynamic Studies (Affinities and Numbers of Sites)
C. Supporting Data and Applications
D. Additional Data
E. Cations
F. Evidence from Electrophoresis
G. Evidence from Conformational Effects
H. Protection against Unfolding
I. Miscellaneous Reports of Small Ion Binding to Proteins
J. Kinetics of Binding Processes
K. Effect of Binding on Subunit Interactions
References
VIII. Protein-Protein Interaction
I. Introduction
II. Quarternary Structure in Proteins
III. Glutamic Dehydrogenase
IV. Tobacco Mosaic Virus Protein
V. Hemerythrin
References
IX. Summary and Conclusions
References
Author Index
Subject Index
Details
- No. of pages:
- 402
- Language:
- English
- Copyright:
- © Academic Press 1969
- Published:
- 1st January 1969
- Imprint:
- Academic Press
- eBook ISBN:
- 9781483220307
About the Authors
Jacinto Steinhardt
Jacqueline A. Reynolds
About the Editors
Bernard Horecker
Nathan O. Kaplan
Julius Marmur
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