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Dynamics and the Problem of Recognition in Biological Macromolecules

  • Book
  • © 1996

Overview

Editors:
  1. Oleg Jardetzky

    1. Stanford University, Stanford, USA

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    You can also search for this editor in PubMed   Google Scholar

  2. Jean-François Lefèvre

    1. ESBS, Université Louis Pasteur, Illkirch Graffenstaden, France

    View editor publications

    You can also search for this editor in PubMed   Google Scholar

Part of the book series: NATO Science Series A: (NSSA, volume 288)

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Table of contents (19 chapters)

  1. Front Matter

    Pages i-viii
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  2. The Cooperative Substructure of Protein Molecules

    • Yawen Bai, S. Walter Englander
    Pages 1-7

  3. NMR Structures of Serine Proteinase Inhibitors LDTI and RBI, and Comparison With X-ray Structures

    • Tad A. Holak, Richard A. Engh
    Pages 9-27

  4. Solution Structure of the Long Neurotoxin LSIII with Possible Implications for Binding to the Acetylcholine Receptor

    • Peter J. Connolly, Alan S. Stern, Jeffrey C. Hoch
    Pages 29-35

  5. NMR Studies of Enzyme-Substrate and Protein-Protein Interactions

    • Gordon C. K. Roberts
    Pages 37-47

  6. The Direct Determination of Protein Structure from Multidimensional NMR Spectra without Assignment

    • R. Andrew Atkinson, Vladimir Saudek
    Pages 49-55

  7. Accuracy of Nuclear Magnetic Resonance Derived Molecular Structures

    • Ricardo González Méndez
    Pages 57-63

  8. What Limits Protein Folding

    • Tobin R. Sosnick, S. Walter Englander
    Pages 65-71

  9. Approaches to the Determination of More Accurate Cross-Relaxation Rates and the Effects of Improved Distance Constraints on Protein Solution Structures

    • Charles G. Hoogstraten, John L. Markley
    Pages 73-111

  10. Protein Dynamics

    • Martin Karplus, Amedeo Caflisch, Andrej Šali, Eugene Shakhnovich
    Pages 113-126

  11. Insights into Protein Dynamics by NMR Techniques

    • Lorna J. Smith, Christopher M. Dobson
    Pages 127-138

  12. Heteronuclear Relaxation and the Experimental Determination of the Spectral Density Function

    • K. T. Dayie, G. Wagner, J.-F. Lefèvre
    Pages 139-162

  13. How Conventional Antigens and Superantigens Interact with the Human MHC Class II Molecule HLA-DR1

    • Ted Jardetzky
    Pages 163-172

  14. Simulating the Dynamics of the DNA Double Helix in Solution

    • Miriam Hirshberg, Michael Levitt
    Pages 173-191

  15. Developments in NMR Structure Determination of Nucleic Acids

    • C. W. Hilbers, S. S. Wijmenga, H. Hoppe, H. A. Heus
    Pages 193-207

  16. Solution Dynamics of the TRP-Repressor Studied by NMR Spectroscopy

    • Oleg Jardetzky, Zhiwen Zheng
    Pages 209-222

  17. A Refined NMR Solution Structure of the POU-Specific Domain of the Human OCT-1 Protein

    • Michel Cox, Niek Dekker, Rolf Boelens, Hans C. van Leeuwen, Peter C. van der Vliet, Robert Kaptein
    Pages 223-236

  18. Applications of Multidimensional Solid-State NMR Spectroscopy to Membrane Proteins

    • A. Ramamoorthy, F. M. Marassi, S. J. Opella
    Pages 237-255

  19. Conformation, Mobility, and Function of the N-Linked Glycan in the Adhesion Domain of Human CD2

    • Gerhard Wagner, Daniel F. Wyss, Johnathan S. Choi, Jing Li, Alex Smolyar, Antonio R. N. Arulanandam et al.
    Pages 257-266

  20. Abstracts

    • Oleg Jardetzky, Jean-François Lefèvre
    Pages 267-299
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Keywords

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.

Editors and Affiliations

  • Stanford University, Stanford, USA

    Oleg Jardetzky

  • ESBS, Université Louis Pasteur, Illkirch Graffenstaden, France

    Jean-François Lefèvre

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