Statistical Mechanics, Protein Structure, and Protein Substrate Interactions

  • Sebastian Doniach

Part of the NATO ASI Series book series (NSSB, volume 325)

Table of contents

  1. Front Matter
    Pages i-ix
  2. Protein Folding Intermediates

    1. Robert L. Baldwin
      Pages 1-6
    2. Patricia A. Jennings, H. Jane Dyson, Peter E. Wright
      Pages 7-18
    3. Michel E. Goldberg, Alain F. Chaffotte
      Pages 19-29
  3. Studies in Protein Stability

  4. Basic Interactions

    1. Themis Lazaridis, Michael E. Paulaitis
      Pages 87-101
  5. Statistical Mechanical Models and Protein States

    1. Ken A. Dill, Klaus M. Fiebig
      Pages 109-113
    2. J. C. Smith, P. Calmettes, D. Durand, M. Desmadril, S. Furois-Corbin, G. R. Kneller et al.
      Pages 135-145
  6. Exploring Conformation Space

    1. Natalya A. Kurochkina, Hong Seok Kang, B. Lee
      Pages 147-157
    2. Niels Grønbech-Jensen, Sebastian Doniach
      Pages 159-164
    3. Ron Elber, Adrian Roitberg, Carlos Simmerling, Robert Goldstein, Gennady Verkhivker, Haiying Li et al.
      Pages 165-191
    4. R. Oomen, M. S. Chappel, M. Klein
      Pages 193-195
  7. NMR Data and Protein Structure

About this book

Introduction

A number of factors have come together in the last couple of decades to define the emerging interdisciplinary field of structural molecular biology. First, there has been the considerable growth in our ability to obtain atomic-resolution structural data for biological molecules in general, and proteins in particular. This is a result of advances in technique, both in x-ray crystallography, driven by the development of electronic detectors and of synchrotron radiation x-ray sources, and by the development ofNMR techniques which allow for inference of a three-dimensional structure of a protein in solution. Second, there has been the enormous development of techniques in DNA engineering which makes it possible to isolate and clone specific molecules of interest in sufficient quantities to enable structural measurements. In addition, the ability to mutate a given amino acid sequence at will has led to a new branch of biochemistry in which quantitative measurements can be made assessing the influence of a given amino acid on the function of a biological molecule. A third factor, resulting from the exponential increase in computing power available to researchers, has been the emergence of a growing body of people who can take the structural data and use it to build atomic-scale models of biomolecules in order to try and simulate their motions in an aqueous environment, thus helping to provide answers to one of the most basic questions of molecular biology: the relation of structure to function.

Keywords

Peptide X-ray development mechanics proteins

Editors and affiliations

  • Sebastian Doniach
    • 1
  1. 1.Stanford UniversityStanfordUSA

Bibliographic information

  • DOI https://doi.org/10.1007/978-1-4899-1349-4
  • Copyright Information Springer-Verlag US 1994
  • Publisher Name Springer, Boston, MA
  • eBook Packages Springer Book Archive
  • Print ISBN 978-1-4899-1351-7
  • Online ISBN 978-1-4899-1349-4
  • Series Print ISSN 0258-1221
  • About this book