Molecular biology has now advanced to the point where it is no longer possible to give a complete review of the available data on the conformational features of proteins. New data keep streaming in, and there is obviously an urgent need for some sort of general treatment of the subject. A systematic treatment of the large amount of data obtained by a great variety of methods on a great variety of objects must be based on the use of models; these should be as simple as possible, should conform to well-established scien tific laws, and at the same time be sufficiently flexible. The validity of the models finally arrived at is then confirmed or otherwise by testing the conclusions arrived at with their aid by means of experiment. After a suitable model has been adopted, it can be used in analyzing the experimental data. Such an analysis may result in one of three possible situations: neither the experi mental results nor their interpretation contradict the proposed model; the experimental results do not contradict the proposed model but their interpretation by the authors does; finally, both the experimental results and their interpretation may be found to be incompatible with the fundamental principles underlying the proposed model. The first situation is clearly the most desirable, and presents no difficulties.

Inhalt
1 / The Properties of Water.- 1.1. Pure Water.- 1.2. Water in Model Systems.- 2 / Principles and Implications of the Dynamic Model of Behavior of Proteins in Aqueous Media.- 2.1. Description of the Properties of Proteins in Terms of the Dynamic Model.- 2.2. A Description of the Properties of Membranes in Terms of the Dynamic Model.- 3 / Conformational Mobility of Proteins.- 3.1. Studying Hydrated Biopolymers by IR Spectroscopy.- 3.2. Fundamental Principles of Hydrogen Exchange Method.- 3.3. Results Obtained by Hydrogen Exchange and Proteolytic Studies.- 3.4. Fundamental Principles and Applications of the NMR Method.- 3.5. Gamma-Resonance Spectroscopy and its Applications.- 3.6. The Method of Spin Label and its Application.- 3.7. Application of Luminescence to the Study of Protein Dynamics.- 3.8. Results of X-Ray Diffraction Studies of Protein Mobility.- 4 / Interaction Between Proteins and Water.- 4.1. Hydration of Biopolymers and Methods of its Study.- 4.2. Protein Cavities (Clefts) and their Interaction with Water.- 4.3. The Dynamics of Water-Protein Interaction.- 5 / Effect of Perturbing Agents on the Dynamic Properties of Proteins.- 5.1. Changes in the Conformation and Stability of Proteins Brought about by Perturbing Agents.- 5.2. Effect of Temperature on Protein Dynamics and on the Interaction between the Protein and the Surrounding Solvent.- 5.3. Ultrasonic Action.- 6 / Dynamic Model of Association and Dissociation of Specific Complexes.- 6.1. Effect of Complex Formation on the Stability of the Protein.- 6.2. Effect of Complex Formation on Dynamic Properties of Proteins.- 6.3. Immunoglobulins.- 6.4. Cytochrome c.- 6.5. Myoglobulin.- 6.6. Hemoglobin.- 7 / Dynamic Model of Protein Behavior and Mechanism of Enzymatic Function.- 7.1. A Possible Connection between theKinetic and Conformational Properties of Enzymes.- 7.2. Comparison between the Dynamic Model of Enzymatic Activity and Other Models of Enzymatic Catalysis.- 7.3. Relaxational Properties of Enzymes.- 7.4. Effect of Perturbing Agents on Enzymatic Activity.- 7.5. Action of D2 O on Enzymes.- 7.6. Glyceraldehyde-3-Phosphate Dehydrogenase.- 7.7. Transaminase.- 7.8. Myosin.- 7.9. Lysozyme.- 7.10. ?-Chymotrypsin and Pepsin.- 7.11. Study of Reactions Involving Papain at Low Temperature.- 7.12. Allosteric Enzymes.- 8 / Interactions between Macromolecules of Different Types and Proteins and Cells in Aqueous Media.- 8.1. Effect of Polymers on the Flexibility of Antibodies in Complex with Spin-labeled Hapten at Different Temperatures.- 8.2. Effect of Proteins on the Flexibility of Antibodies and Oxyhemoglobin.- 8.3. Effect of Thermality Induced Transitions of Human Serum Albumin on the Mobility of the Subunits of Spin-labeled Oxyhemoglobin.- 8.4. Effect of Polymers and Proteins in Different Ligand States of Active Sites on the Properties of the Solvent.- 8.5. Interaction between Serum Proteins and Cells.- Conclusion.- References.- Index of Authors.- Index of Subjects.