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An evaluation of the combined use of nuclear magnetic-resonance and distance geometry for the determination of protein conformations in solution

Academic Article
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Overview

authors

  • Havel, T. F.
  • Wuthrich, Kurt

publication date

  • 1985

journal

  • Journal of Molecular Biology  Journal

abstract

  • An evaluation of the potential of nuclear magnetic resonance (n.m.r.) as a means of determining polypeptide conformation in solution is performed with the aid of a new distance geometry program which is capable of computing complete spatial structures for small proteins from n.m.r. data. Ten sets of geometric constraints which simulate the results available from n.m.r. experiments of varying precision and completeness were extracted from the crystal structure of the basic pancreatic trypsin inhibitor, and conformers consistent with these constraints were computed. Comparison of these computed structures with each other and with the original crystal structure shows that it is possible to determine the global conformation of a polypeptide chain from the distance constraints which are available from n.m.r. experiments. The results obtained with the different data sets also provide a standard by which the quality of protein structures computed from n.m.r. data can be evaluated when no crystal structure is available, and indicate directions in which n.m.r. experiments for protein structure determination could be further improved.

subject areas

  • Animals
  • Aprotinin
  • Cattle
  • Crystallization
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Protein Conformation
  • Software
  • Solutions
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/0022-2836(85)90346-8

PubMed ID

  • 2582141
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Additional Document Info

start page

  • 281

end page

  • 294

volume

  • 182

issue

  • 2

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