Chemical Relaxation in Molecular Biology

The development of an area of scientific research is a dynamic process with its own kinetic equations and its own physical mech anism. The study of fast chemical interactions and transformations is such an area, and while it is tempting to draw analogies or to speculate about the simplest model system, the lack of ade quately averaged observables is an annoying obstacle to such an undertaking. Sciences suffering from such conditions usually avoid quantitative models, be they primitive or complex. Instead, they prove their point by "case histories". Chemical relaxation kinetics started as an offspring of research in acoustics. In some aqueous ionic solutions anomalous acoustic absorption had been observed. A systematic study traced the cause of this absorption, showing that the covered frequency range and the intensity of the absorption were related in a predictable manner to the rate at which ions can interact and form structures differing in volume from the non interacting species. The step from this experimental observation and its correct, non trivial explanation to the discovery that all fast chemical pro cesses must reveal themselves quantitatively in the relaxation rate of a perturbed equilibrium state, and that perturbation para meters other than sound waves can be used for its exploitation, was made by MANFRED EIGEN in 1954. The foresightedness of K.F.

Auteur
Peter Schuster, geboren 1957, lehrte von 2006 bis 2010 als Professor an der Universität des Saarlandes. 2009 war er "Professeur inivité" an der "École des Hautes Études en Sciences Sociales" in Paris. Seit 2011 ist er Professor für die Geschichte des Mittelalters und der Frühen Neuzeit an der Universität Bielefeld.

Contenu
Theory and Simulation of Chemical Relaxation Spectra.- I. Introduction.- References.- Concentration Correlation Analysis and Chemical Kinetics.- I. Introduction.- II. Properties of Thermodynamic Fluctuations.- III. Measurement of Number Fluctuations.- IV. Summary and Conclusions.- References.- Dynamics of Substitution at Metal Ions.- I. Introduction.- II. Formation of 1:1 Complexes with Small Ligands.- III. Formation of 1:1 Complexes with Large Ligands.- IV. The Effect of Bound Ligands.- V. Summary.- References.- Dynamics of Proton Transfer in Solution.- I. Introduction.- II. Theoretical Background of Proton Transfer.- III. Proton Transfer in Aqueous Solution.- IV. Proton Transfer in Non-Aqueous Solvents.- V. Biochemical Model Studies.- VI. Polypeptides and Proteins.- VII. Experimental Techniques.- VIII. Conclusion.- IX. Other Review Articles and Books on Proton Transfer..- References.- Elementary Steps of Base Recognition and Hdlix-Coil Transitions in Nucleic Acids.- I. Introduction.- II. Elementary Steps of Bases Stacking.- III. Ion Condensation to Polynucleotides.- IV. Recognition of Monomer Bases on a Polymer Template..- V. Helix-Coil Transition of Oligo(A)•Oligo(U).- VI. The Influence of GC Base Pairs.- VII. Specific Effects in Helix Loops.- VIII. Dynamics of Polymer Helix-Coil Transitions.- IX. Rate and Specificity of Genetic Information Transfer.- X. Summary.- References.- Structural Dynamics of tRNA. A Fluorescence Relaxation Study of tRNA.- I. Introduction.- II. Fluorescent Probes for the Structure of tRNA.- III. Pulsed Fluorescence Measurements.- IV. Measurements Under Stationary Excitation.- V. Measurements of Chemical Rates.- VI. A Model for Aliosteric Conformations of tRNA.- VII. Conformational States of tRNA with Regard to the Biological Role of tRNA.-References.- Chemical Relaxation Kinetic Studies of E. eoli RNA Polymerase Binding to Poly[d(A-T)] Using Ethidium Bromide as a Fluorescence Probe.- I. Introduction.- II. Experimental Procedures and Data Analysis.- III. Excluded Site Binding of Ethidium Bromide to Poly [d (A-T)].- IV. Relaxation Kinetics of Ethidium Bromide and Poly [_d (A-T) J in the Presence of RNA Polymerase.- V. Conclusions.- VI. Appendix. On the Derivation of General Equations for Relaxation Kinetics of Systems with Excluded Binding.- References.- Protein Folding and Unfolding.- I. Introduction.- II. Time-Independent Phenomena.- III. Slow Temperature-Jump Methods.- IV. Kinetics of Unfolding and Refolding.- V. Theoretical Approach to the Kinetics of Folding.- Kinetics of Antibody-Hapten Interactions.- I. Introduction.- II. The Kinetics of the Association Step.- III. Kinetic Expression of the Elementary Interactions.- IV. Conformational Transitions Induced by Hapten Binding.- References.- Glutamate Dehydrogenase Self-Assembly. An Application of the Light Scattering Temperature-Jump Technique to the Study of Protein Aggregation.- I. Introduction.- II. Structural Features.- III. Thermodynamics of Self-Assembly.- IV. Scattered Light Detection in Chemical Relaxation Experiments.- V. Kinetics of Self-Assembly.- References.- Dynamic Aspects of Carrier-Mediated Cation Transport Through Membranes.- I. Introduction and General Considerations.- II. Kinetic Studies on Lipid Bilayer Membranes.- III. Elementary Steps Involved in Carrier-Mediated Cation Transport.- IV. Comparison of the Dynamic Aspects of Cation Carriers Bound to Membranes and in Homogeneous Solution.- V. Summary.- References.