Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Secondary structure in the solution conformation of the proteinase inhibitor-iia from bull seminal plasma by nuclear magnetic-resonance

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Williamson, M. P.
  • Marion, D.
  • Wuthrich, Kurt

publication date

  • 1984

journal

  • Journal of Molecular Biology  Journal

abstract

  • Nuclear magnetic resonance data on the protease inhibitor IIA from bull seminal plasma were used to determine the secondary structure elements in the solution conformation of the protein. The experimental data were obtained from analyses of two-dimensional 1H nuclear magnetic resonance spectra at 500 and 360 MHz and include details of inter-residue nuclear Overhauser enhancements, vicinal spin-spin coupling constants and the sequence location of slowly exchanging amide protons. Accurate measurement of coupling constants and reliable assignments of nuclear Overhauser enhancements were facilitated by the use of absorption mode two-dimensional spectroscopy and large data matrices. It is shown that the peptide backbone is extended from residues 4 to 7, followed by a poorly defined helical region from residues 8 to 13 with a marked change of direction at residue Phe10. Residues 15 to 19 are extended and there is a kink at residue Glu20. Residues 22 to 27 form the central strand of a triple-stranded antiparallel beta-sheet, of which the other two strands are residues 29 to 33 and 49 to 53. Residues 34 to 46 form a helix. The tight turn in the beta-sheet is of type I geometry, and there is a beta-bulge at residue His53.

subject areas

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Male
  • Prostatic Secretory Proteins
  • Protease Inhibitors
  • Protein Conformation
  • Proteins
  • Semen
  • Seminal Plasma Proteins
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/0022-2836(84)90125-6

PubMed ID

  • 6699915
scroll to property group menus

Additional Document Info

start page

  • 341

end page

  • 359

volume

  • 173

issue

  • 3

©2019 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support