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Calibration of the angular-dependence of the amide proton-c-alpha proton coupling-constants, 3jhn-alpha, in a globular protein - use of 3jhn-alpha for identification of helical secondary structure

Academic Article
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Overview

authors

  • Pardi, A.
  • Billeter, M.
  • Wuthrich, Kurt

publication date

  • 1984

journal

  • Journal of Molecular Biology  Journal

abstract

  • The vicinal amide proton-C alpha proton spin-spin coupling constants, JHN alpha, in the globular protein basic pancreatic trypsin inhibitor (BPTI) have been measured using phase-sensitive correlated spectroscopy at high digital resolution. In conjunction with the crystal structure of BPTI, these data were used to calibrate the correlation between 3JHN alpha and the dihedral angle phi. The resulting "BPTI curve" is 3JHN alpha = 6.4 cos2 theta - 1.4 cos theta + 1.9 (theta = [phi - 60 degrees]). It is further shown that measurement of the spin-spin couplings 3JHN alpha presents an independent, reliable method for identification of the location of helical structure in the amino acid sequence of proteins.

subject areas

  • Amides
  • Aprotinin
  • Crystallization
  • Magnetic Resonance Spectroscopy
  • Protein Conformation
  • Protons
  • Spectrum Analysis
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/0022-2836(84)90035-4

PubMed ID

  • 6084720
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Additional Document Info

start page

  • 741

end page

  • 751

volume

  • 180

issue

  • 3

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