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Statistical mechanics and stability of macromolecules : application to bond disruption, base pair separation, melting, and drug dissociation of the DNA double helix / Earl Prohofsky.

By: Material type: TextTextPublisher: Cambridge : Cambridge University Press, 1995Description: 1 online resource (x, 227 pages) : digital, PDF file(s)Content type:
  • text
Media type:
  • computer
Carrier type:
  • online resource
ISBN:
  • 9780511524721 (ebook)
Other title:
  • Statistical Mechanics & Stability of Macromolecules
Subject(s): Additional physical formats: Print version: : No titleDDC classification:
  • 574.87/3282 20
LOC classification:
  • QP624.5.S73 P76 1995
Online resources: Summary: 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 co-operative transitions needed to explain helix melting. A new theoretical approach for executing macromolecule calculations is developed. In particular, the author devises a method for describing chemical bond disruption in these large systems, which are then used to determine when the helix melts and how drugs can dissociate from the helix. Melting temperatures are found to be in excellent agreement with experimental observations. The book will be of interest to biomolecular dynamics researchers, especially to graduate students in biological physics, theoretical chemistry and molecular biology.
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Title from publisher's bibliographic system (viewed on 05 Oct 2015).

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 co-operative transitions needed to explain helix melting. A new theoretical approach for executing macromolecule calculations is developed. In particular, the author devises a method for describing chemical bond disruption in these large systems, which are then used to determine when the helix melts and how drugs can dissociate from the helix. Melting temperatures are found to be in excellent agreement with experimental observations. The book will be of interest to biomolecular dynamics researchers, especially to graduate students in biological physics, theoretical chemistry and molecular biology.

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