Dynamics and the Problem of Recognition in Biological Macromolecules

  • Oleg Jardetzky
  • Jean-François Lefèvre

Part of the NATO ASI Series book series (NSSA, volume 288)

Table of contents

  1. Front Matter
    Pages i-viii
  2. Yawen Bai, S. Walter Englander
    Pages 1-7
  3. Tobin R. Sosnick, S. Walter Englander
    Pages 65-71
  4. Martin Karplus, Amedeo Caflisch, Andrej Šali, Eugene Shakhnovich
    Pages 113-126
  5. Lorna J. Smith, Christopher M. Dobson
    Pages 127-138
  6. Miriam Hirshberg, Michael Levitt
    Pages 173-191
  7. C. W. Hilbers, S. S. Wijmenga, H. Hoppe, H. A. Heus
    Pages 193-207
  8. Oleg Jardetzky, Zhiwen Zheng
    Pages 209-222
  9. Michel Cox, Niek Dekker, Rolf Boelens, Hans C. van Leeuwen, Peter C. van der Vliet, Robert Kaptein
    Pages 223-236
  10. A. Ramamoorthy, F. M. Marassi, S. J. Opella
    Pages 237-255
  11. Gerhard Wagner, Daniel F. Wyss, Johnathan S. Choi, Jing Li, Alex Smolyar, Antonio R. N. Arulanandam et al.
    Pages 257-266
  12. Oleg Jardetzky, Jean-François Lefèvre
    Pages 267-299
  13. Back Matter
    Pages 301-311

About this book


From within complex structures of organisms and cells down to the molecular level, biological processes all involve movement. Muscular fibers slide on each other to activate the muscle, as polymerases do along nucleic acids for replicating and transcribing the genetic material. Cells move and organize themselves into organs by recognizing each other through macromolecular surface-specific interactions. These recognition processes involve the mu­ tual adaptation of structures that rely on their flexibility. All sorts of conformational changes occur in proteins involved in through-membrane signal transmission, showing another aspect of the flexibility of these macromolecules. The movement and flexibility are inscribed in the polymeric nature of essential biological macromolecules such as proteins and nucleic acids. For instance, the well-defined structures formed by the long protein chain are held together by weak noncovalent interac­ tions that design a complex potential well in which the protein floats, permanently fluctuating between several micro- or macroconformations in a wide range of frequencies and ampli­ tudes. The inherent mobility of biomolecular edifices may be crucial to the adaptation of their structures to particular functions. Progress in methods for investigating macromolecular structures and dynamics make this hypothesis not only attractive but more and more testable.


DNA DNA double helix cells polymer protein proteins spectroscopy

Editors and affiliations

  • Oleg Jardetzky
    • 1
  • Jean-François Lefèvre
    • 2
  1. 1.Stanford UniversityStanfordUSA
  2. 2.ESBS, Université Louis PasteurIllkirch GraffenstadenFrance

Bibliographic information

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