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Correlations between internal mobility and stability of globular-proteins

Academic Article
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Overview

authors

  • Wuthrich, Kurt
  • Wagner, G.
  • Richarz, R.
  • Braun, W.

publication date

  • 1980

journal

  • Biophysical Journal  Journal

abstract

  • The recent work is surveyed which leads to the suggestions that the conformation of globular proteins in solution corresponds to a dynamic ensemble of rapidly interconverting spatial structures, that clusters of hydrophobic amino acid side chains have an important role in the architecture of protein molecules, and that mechanistic aspects of protein denaturation can be correlated with internal mobility seen in the native conformation. These conclusions resulted originally from high resolution 1H nuclear magnetic resonance (NMR) studies of aromatic ring mobility, exchange of interior amide protons and thermal denaturation of the basic pancreatic trypsin inhibitor and a group of related proteins. Various new approaches to further characterize proteins in solution have now been taken and preliminary data are presented. These include computer graphics to outline hydrophobic clusters in globular protein structures, high resolution 1H-NMR experiments at variable hydrostatic pressure and 13C-NMR relaxation measurements. At the present early stage of these new investigations it appears that the hydrophobic cluster model for globular proteins is compatible with the data obtained.

subject areas

  • Amino Acids
  • Drug Stability
  • Globulins
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Protein Conformation
  • Trypsin Inhibitor, Kazal Pancreatic
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Identity

PubMed Central ID

  • PMC1327351

International Standard Serial Number (ISSN)

  • 0006-3495

Digital Object Identifier (DOI)

  • 10.1016/S0006-3495(80)84989-7

PubMed ID

  • 7248460
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Additional Document Info

start page

  • 549

end page

  • 560

volume

  • 32

issue

  • 1

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