Use of the Neutron Diffraction—H/D Exchange Technique to Determine the Conformational Dynamics of Trypsin

  • Anthony A. Kossiakoff
Part of the Basic Life Sciences book series (BLSC, volume 27)


A number of structural and chemical investigations (1–6) have shown that, even though protein molecules possess a high degree of secondary structure, they have numerous component segments which exhibit substantial fluctuations from their native conformations. A majority of these fluctuations represent a localized denaturation of small portions of the structure and result from the natural equilibrium between protein-protein and protein-solvent interactions. Although most of these fluctuations probably have little direct effect on the regions responsible for functional activity of the protein, a growing body of evidence indicates that conformational change is an important ingredient in a significant number of biological processes (7–10).


Neutron Diffraction Amide Proton Regional Melting Peptide Proton Amide Peptide 
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Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Anthony A. Kossiakoff
    • 1
  1. 1.Brookhaven National LaboratoryUptonUSA

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