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Protein-Solvent Interactions - Roger Gregory

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Protein-Solvent Interactions

Name: Protein-Solvent Interactions
Brand: MARCEL DEKKER INC
Price: 645.9 AUD
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By: Roger Gregory (Editor)

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Hardcover | 4 January 1995 | Edition Number 1

At a Glance

Hardcover
570 Pages

Dimensions(cm)
22.9 x 15.2 x 3.18

Hardcover

RRP $777.00

$645.90

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This practical resource covers the latest advances in the interactions of proteins with their solvent environment and provides fundamental physical information useful for the application of proteins in biotechnology and industrial processes. It discusses in detail structural, dynamic, and thermodynamic aspects of protein hydration as well as proteins in aqueous and organic solvents as they relate to protein function, stability, and folding.

Industry Reviews

." . .a broad and much-needed survey of biophysical aspects of the interplay between proteins and their solvent. . . . . .uniformly well-written. . .of value to anyone with an active interest in the physical chemistry of proteins." ---FEBS Letters

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Non-Fiction Engineering & Technology Biochemical Engineering Biotechnology Science Chemistry Medicine Other Branches of Medicine Pharmacology Biology, Life Sciences Biochemistry Proteins

Preface	p. iii
Contributors	p. xvii
The New Paradigm for Protein Research	p. 1
Introduction	p. 1
Purposes	p. 1
Confusing Biology with Chemistry	p. 8
Supporting Evidence	p. 9
Protein Structure	p. 10
Information from B Factors	p. 10
Observations Based on B Factors	p. 12
Information from Proton-Exchange Studies	p. 28
Information About Groups from Evolution and Genetics	p. 36
Information from Density Data	p. 39
How Substructures Determine Gestalt Structure and Properties	p. 39
Genetic Stability	p. 39
Kinetic Stability	p. 40
Thermodynamic Stability	p. 45
"Molten-Globule" Conformation States	p. 53
Structural Dependence of Common Experimental Observables	p. 54
Some Devices that Became Possible After the Discovery of the Knot-Matrix Construction Principle	p. 56
Modular Construction of Knot-Matrix Proteins	p. 56
Expansion-Contraction Processes	p. 56
Free Volume and Dielectric Constant	p. 57
The "Pairing Principle"	p. 58
"Completing the Knot"	p. 59
Protein Activity Coefficients: Gibbs-Duhem Consequences	p. 62
Intermolecular Communication Through Surfaces	p. 67
Some Thermodynamic Topics of Special Importance for Biology	p. 69
Weak Relationship Between Free Energy and Its Temperature and Pressure Derivatives	p. 69
Enthalpy-Entropy Compensation Behavior	p. 75
Conformational Dynamics and "Dynamic Matching"	p. 82
The Facts	p. 82
Protein-Protein Association	p. 91
The Oxygen-Binding Mechanism of Hemoglobins	p. 94
Enzyme Mechanisms: Updating the Rack Mechanism	p. 100
The Kunitz Proteinase Inhibitors	p. 117
The Immune Reaction	p. 118
Dynamical Aspects of Protein Electrostatic Potentials	p. 123
The Next Level of Complexity	p. 123
What Is the Atomic Description of a Knot?	p. 123
What Factors Are Responsible for the Stability of Knots?	p. 124
Gestalt Versus Local Fields	p. 126
Summary	p. 129
Thermodynamics in the Biosphere	p. 129
The Evolution of Devices	p. 130
Function Follows Form?	p. 131
Consequences for the Immediate Future of Protein Chemistry	p. 133
Hypotheses Based on the Knot-Matrix Principle	p. 134
References	p. 136
Solvent Interactions with Proteins as Revealed by X-Ray Crystallographic Studies	p. 143
Introduction	p. 143
Solvent Content of Protein Crystals	p. 144
Crystallographic Location of Solvent	p. 145
The Crystallographic Method	p. 145
Identification and Refinement of Solvent Sites	p. 146
Chemical Identity of Solvent Molecules	p. 150
Patterns of Solvent Structure	p. 151
The General Picture	p. 151
Hydration of Protein Groups	p. 154
Internal Solvent Molecules	p. 157
Surface Solvent Structure	p. 162
Association with Secondary Structures	p. 167
Solvent in Active Sites	p. 172
Significance of Bound Solvent	p. 174
Conservation of Solvent Sites	p. 174
Contributions to Stability	p. 178
Functional Roles of Solvent Molecules	p. 180
Bound Ions and Other Solvent Molecules	p. 182
Conclusions	p. 185
References	p. 185
Protein Hydration and Glass Transition Behavior	p. 191
Introduction	p. 191
Preparation of Solid State Samples	p. 193
Adsorption of Water Vapor by Proteins: The Sorption Isotherm	p. 193
Conventional Sorption Isotherms	p. 195
Site Heterogeneity and Conformational Perturbations	p. 198
Sorption Hysteresis	p. 201
Identification and Coverage of Sorption Sites and Some Critical Hydration Levels in the Sorption Isotherm	p. 205
Infrared Spectroscopic Studies of Protein Hydration	p. 206
Heat Capacity as a Function of Hydration	p. 207
Enzyme Activity	p. 210
Proton Percolation	p. 211
Nonfreezing Water	p. 214
The Effect of Hydration on Thermal Stability	p. 215
Protein Surface Areas and Monolayer Coverage	p. 217
Hydration-Induced Conformational Changes	p. 217
Solid State [superscript 13]C NMR Studies of Protein Hydration	p. 218
An X-Ray Diffraction Study of a Dehydrated Protein	p. 219
FTIR Studies of Dehydration-Induced Conformational Transitions	p. 220
Effect of Hydration on Protein Dynamics	p. 221
Spectroscopic Methods	p. 221
Hydrogen Isotope Exchange	p. 224
Positron Annihilation Lifetime Spectroscopy	p. 225
Glass Transitions in Proteins	p. 227
Glass Transition Behavior in Polymers	p. 227
Free Volume in Glass Transition Theory	p. 230
The 200 K Transition in Fully Hydrated Proteins	p. 232
Hydration Dependence of Glass Transition Temperatures	p. 233
Hysteresis Effects	p. 236
Dynamically Distinct Structural Classes in Globular Proteins	p. 237
Evidence from Hydrogen Isotope Exchange	p. 238
The Basis of Knot Formation	p. 242
The Connection Between Hydrogen Exchange Properties and Glass Transition Behavior	p. 245
"Molten Globule" and Cold-Denatured States	p. 249
Protein Folding	p. 249
Conclusions	p. 257
References	p. 259
Dielectric Studies of Protein Hydration	p. 265
Introduction	p. 265
Dielectric Theory and Measurements	p. 266
Experimental Results	p. 273
Protein Solutions	p. 273
Solid State Studies	p. 275
Water as Plasticizer	p. 277
Proton Conduction Effects	p. 281
Concluding Remarks	p. 285
References	p. 286
Protein Dynamics: Hydration, Temperature, and Solvent Viscosity Effects as Revealed by Rayleigh Scattering of Mossbauer Radiation	p. 289
Introduction	p. 289
Background of RSMR Technique, Basic Expressions, and Approximations	p. 290
Hydration Dependencies of the Elastic RSMR Fractions and RSMR Spectra	p. 296
Solvent Composition and Viscosity Dependencies of the Elastic RSMR Fractions	p. 300
Temperature Dependencies of the Elastic RSMR Fraction and RSMR Spectra	p. 305
Angular Dependencies of Inelastic RSMR Intensities	p. 306
Properties of Protein-Bound Water	p. 309
Dynamical Properties of Hydrated Proteins	p. 314
Principal Conclusions and Outlook	p. 321
References	p. 322
Proteins in Essentially Nonaqueous Environments	p. 327
Introduction	p. 327
"Anhydrous" and Heterogeneous Systems	p. 332
"Anhydrous" and Homogeneous Systems	p. 335
Water/Cosolvent Mixtures	p. 337
Conclusions	p. 339
References	p. 340
Solvent Viscosity Effect on Protein Dynamics: Updating the Concepts	p. 343
Introduction	p. 343
Brownian Dynamics	p. 344
Basics	p. 345
Generalized Approach	p. 349
Free Volume	p. 356
Barrier Crossing	p. 358
Basic Concepts	p. 358
Models	p. 359
Viscosity Effect	p. 363
Kinetic Studies	p. 363
Ultrasonic Studies	p. 364
Why a Power Law?	p. 368
Conclusions	p. 369
References	p. 369
Effect of Solvent on Protein Internal Dynamics: The Kinetics of Ligand Binding to Myoglobin	p. 375
Introduction	p. 375
The Flash Photolysis Experiment	p. 377
The Kinetics of CO Binding to Myoglobin	p. 378
The Surface Barrier	p. 380
The Internal Barriers	p. 382
Conclusion	p. 383
References	p. 384
Solvent Effects on Protein Stability and Protein Association	p. 387
Introduction: A Historic Perspective	p. 387
Protein Folding and Protein-Protein Association	p. 390
Direct and Indirect Interactions	p. 396
Driving Force, Force, and Stability	p. 401
Inventory of Solvent-Induced Effects	p. 407
The Missing Information and How to Obtain It	p. 413
The Solvation Gibbs Energy of the Large Linear Polypeptide Having No Side Chains	p. 413
Solvation of the Backbone of the F Form	p. 414
Loss of the Conditional Solvation Gibbs Energies of the Various Side Chains	p. 414
Pairwise Correlations	p. 415
Higher-Order Correlations	p. 416
Concluding Remarks	p. 417
References	p. 420
Thermodynamic Mechanisms for Enthalpy-Entropy Compensation	p. 421
Introduction	p. 421
Experimental Examples	p. 422
Interaction Mechanisms and Compensation Vector Diagrams	p. 423
Examples of Partial Compensation	p. 425
Thermodynamic Compensation	p. 427
Molecular Species	p. 428
Mathematical Formulation	p. 431
Standard Partial Enthalpies and Entropies in Dilute Solutions	p. 433
Molar-Shift Mechanism	p. 433
Solvation Mechanism	p. 435
Application to Nonpolar Solutes in Water	p. 438
Delphic Dissection of Standard Partial Entropies	p. 439
Concluding Remarks	p. 441
References	p. 442
Preferential Interactions of Water and Cosolvents with Proteins	p. 445
Introduction	p. 445
Cosolvent Control of Protein Solution Stability and State of Dispersion	p. 446
Binding of Cosolvent and Displacement of Reaction Equilibria	p. 446
What Is Binding?	p. 447
Cosolvent Effects on Equilibria Relative to Water	p. 448
Relation Between Preferential Interactions and Transfer Free Energy	p. 449
Thermodynamic Definition of Binding	p. 449
Binding Is Replacement of Water by Ligand at a Site	p. 450
The Wyman Slope Is the Change in Thermodynamic Interaction	p. 451
Relation Between Transfer Free Energy and Preferential Interaction	p. 452
How Transfer Free Energy Modulates Protein Reactions	p. 453
Precipitation	p. 453
Structure Stabilization--Destabilization	p. 455
Why Precipitants Are Not Necessarily Stabilizers	p. 461
Preferential Interactions and Binding at Sites	p. 461
Classical Site Binding Theory	p. 462
Inadequacy of the Site Binding Treatment	p. 462
Preferential Binding as Exchange at Sites: Weak and Strong Binding	p. 463
Preferential Binding as the Balance Between Water and Ligand Binding to a Protein: Meaning of Zero "Binding"	p. 465
Meaning of Thermodynamic Indifference	p. 467
Relation Between Global Preferential Interactions and Exchange at Sites	p. 467
Direct Site Occupancy Measurements Cannot Define the Thermodynamic Interaction	p. 470
Weak Effects as Results of Strong Interactions at Sites	p. 471
Meaning of Sites in Weak Binding	p. 474
Why Are Some Cosolvents Preferentially Excluded from Protein?	p. 475
Conclusion: Competition, Compensation, Binding--Exclusion Balance	p. 478
References	p. 479
Thermodynamic Nonideality and Protein Solvation	p. 483
Introduction	p. 483
Quantitative Interpretation of Partial Specific Volumes	p. 484
Traditional Approach	p. 484
Choice of Concentration Scale	p. 486
Direct Thermodynamic Interpretation	p. 489
Equivalence of Treatments	p. 491
Virial Coefficients from Density Measurements	p. 492
Protein--Small Nonelectrolyte Systems	p. 493
Osmolytes as Inert Solute	p. 495
Excluded Volume Interpretation	p. 495
Consideration of Small Solutes as Effective Spheres	p. 496
Interpretation of Isopiestic Measurements	p. 496
Freezing Point Depression Data	p. 500
Frontal Gel Chromatography of Sucrose	p. 500
Validity of the Proposition	p. 502
Effective Thermodynamic Radii of Globular Proteins	p. 503
Evaluation from Self-Covolume Measurements	p. 504
Evaluation from Protein--Small Solute Covolume	p. 507
Relationship to the Stokes Radius	p. 508
Effects of Small Solutes on Protein Isomerization	p. 510
pH-Induced Unfolding of Proteins	p. 512
Ligand-Induced and Preexisting Isomerizations	p. 513
Thermal Unfolding of Proteins	p. 515
Concluding Remarks	p. 516
References	p. 518
Molecular Basis for Protein Separations	p. 521
Introduction	p. 521
Protein Reactivity and Conformation Governance in Separations	p. 524
The Plasma Albumin Prototype: Conformation Behavior, Reactivity Toward Ligands, Consequences in Coprecipitation, and Cocrystallization	p. 526
Salt Counterion Contraction of Proteins from Acid-Expanded Conformation	p. 528
Cocrystallization of Proteins with Inorganic and Organic Ionic Ligands	p. 530
Water Inside, Water Outside Proteins	p. 533
Protein Precipitation from Four-Carbon Cosolvent, t-Butanol	p. 536
Matrix Coprecipitation by Organic Ion Ligands	p. 540
Inorganic and Organic Ion-Binding Thermochemistry	p. 546
References	p. 550
Index	p. 555
Table of Contents provided by Ingram. All Rights Reserved.

Protein-Solvent Interactions

At a Glance

Hardcover

Industry Reviews

Shipping

How to return your order

Defective items

You Can Find This Book In

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