Softcover reprint of the original 1st ed. 1994, X, 150 pp. 58 figs.
Springer eBooks may be purchased by end-customers only and are sold without copy protection (DRM free). Instead, all eBooks include personalized watermarks. This means you can read the Springer eBooks across numerous devices such as Laptops, eReaders, and tablets.
You can pay for Springer eBooks with Visa, Mastercard, American Express or Paypal.
After the purchase you can directly download the eBook file or read it online in our Springer eBook Reader. Furthermore your eBook will be stored in your MySpringer account. So you can always re-download your eBooks.
Proteins constitute the working-class molecules of the cell. Hence, understanding the way they act is a prerequisite for understanding how a cell functions and how life evolves. Aspects such as the protein-ligand relationship, recognition, protein evolution by point mutation, enzyme-substrate interactions, behaviour of an enzyme in a living cell, control and dynamics of enzyme networks as well as the physico-chemical background of enzyme actions and multi-enzyme complexes are comprehensively treated in this volume.
Dynamics of Enzyme Reactions and Metabolic Networks in Living Cells. A Physico-Chemical Approach.- 1. Introduction.- 2. Flows and forces, diffusion, partition of mobile ions by charged matrices.- 3. Compartmentalization of enzyme reactions and the energy metabolism of the cell.- 4. Coupling between reactant diffusion and bound enzyme reaction rate.- 5. Electric partitioning of ions and reaction rate of bound enzyme systems.- 5.1. Electrostatic co-operativity of a bound enzyme system.- 5.2. Spatial organization of fixed charges and enzyme molecules as a source of co-operativity.- 6. An example of enzyme behaviour in organized biological systems: the dynamics of enzymes bound to plant cell walls.- 7. Control and dynamics of enzyme networks.- 7.1. Control of a linear metabolic network.- 7.2. Dynamic organization of a metabolic cycle in homogeneous phase.- 7.3. Dynamic organization of a metabolic cycle at the surface of a charged membrane.- 8. Control of multi-enzyme complexes.- 8.1. Generalized microscopic reversibility and multi-enzyme complexes.- 8.2. The stoichiometry of polypeptide chains in multi-enzyme complexes.- 8.3. The principles of structural kinetics of oligomeric enzymes and of multi-enzyme complexes.- 8.4. Thermodynamics of the alteration of the kinetic behaviour of an oligomeric enzymes within a multi-enzyme complex.- 9. General Conclusions.- References.- Microbial and Genetic Approaches to the Study of Structure-Function Relationships of Proteins.- 1. Introduction.- 2. Protein-ligand and protein-substrate interactions.- 2.1. The recognition problem.- 2.2. Conformational selection by ligand interaction.- 2.3. Protein dynamics and simulation.- 3. Protein evolution by point mutation.- 3.1. The suppressor approach: position-specific design of the substitution matrix.- 3.2. Interdependence of residues located in the hydrophobic core.- 3.3. Essential residues revisited.- 3.4. What is a neutral position?.- 4. Protein evolution by rearrangements of combinatorial domains.- 4.1. Acquiring and integrating new domain(s).- 4.2. Protein secretion in Gram-negative bacteria.- 4.2.1. Domain recruitment as a strategy for acquiring a new function.- 4.2.2. Domain-domain interaction as a strategy for self and non-self recognition.- 5. Conclusion and perspectives.- References.- Recent Progress in Studies of Enzymatic Systems in Living Cells.- 1. Introduction: Why study the behaviour of enzymes in single living cells?.- 1.1. Some words about fluorescence.- 1.2. Practical consequences.- 2. Tools available for studying the behavior of enzymes in single living cells.- 2.1. Instrumentation.- 2.1.1. Fluorescence anisotropy of cells suspension.- 2.1.2. Flow cytometry.- 2.1.3. Microfluorometry (spectral mode).- 2.1.4. Microfluorometry (topographic mode).- 2.1.5. Videomicrofluorometry.- 2.1.6. Life time measurements (decay of intensity and phase fluorometry).- 2.2. Progress in software and modelization.- 2.2.1. Spectral resolution.- 2.2.2. Correlation with biochemical conventional data.- 3. What next?.- 4. General conclusion.- References.