Statistical Mechanics and Stability of Macromolecules: Application to Bond Disruption, Base Pair Separation, Melting, and Drug Dissociation of the DNA Double Helix

by Earl Prohofsky

Overview

This book develops a statistical mechanical analysis of the stability of biological macromolecules. The author's approach is valid both for the long time-scale needed for DNA bond disruption, and also for highly cooperative transitions needed to explain helix melting. Prohofsky develops a new theoretical approach for executing macromolecule calculations. In particular the author devises a method for describing chemical bond disruption in these large systems, which is then used to determine when the helix melts and how drugs can dissociate from the helix. The author finds melting temperatures to be in excellent agreement with experimental observations.

Product Details

ISBN-13:	9780521451840
Publisher:	Cambridge University Press
Publication date:	07/28/1995
Edition description:	New Edition
Pages:	240
Product dimensions:	6.14(w) x 9.21(h) x 0.55(d)

Table of Contents

Preface; 1. Introduction; 2. Macromolecular stability; 3. Lattice dynamics; 4. Effective phonon theory; 5. Premelting disrupted chemical bonds; 6. Co-operative melting; 7. Strained chemical bonds: salt and pressure effects; 8. Bond disruption and conformation change: B to Z confirmation change in DNA; 9. Hydration effects: structural water; 10. Helix with daunomycin intercalated: increased helix stability and daunomycin-DNA bonding constant; 11. Non repeating DNA; 12. Cutting and splicing: junctions, inserts and the replicating fork; 13. Interaction between a helix and a single attached molecule; 14. Energy considerations in bond opening; Appendix 1; Appendix 2; Appendix 3. Index

Editorial Reviews

Develops a statistical mechanical analysis of the stability of biological macromolecules that is valid both for the long time scale needed for DNA bond disruption and for the highly cooperative transitions needed to explain helix melting. Devises a method for describing chemical bond disruption in such systems, and uses that to determine when the helix melts and how drugs can dissociate from the helix. Then shows how to account for environmental variables and how to perform calculations on specific structures embedded in a large helix and on the dynamic effects of enzyme attachments. For researchers and graduate students in biological physics, theoretical chemistry, and molecular biology. Annotation c. Book News, Inc., Portland, OR (booknews.com)

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