Scripps VIVO scripps research logo

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

High-resolution nuclear magnetic-resonance studies of the conformation and orientation of melittin bound to a lipid-water interface

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

Overview

authors

  • Brown, L. R.
  • Braun, W.
  • Kumar, A.
  • Wuthrich, Kurt

publication date

  • 1982

journal

  • Biophysical Journal  Journal

abstract

  • Previously, the size and stoichiometry of mixed micelles of perdeuterated dodecylphosphocholine and melittin were characterized and the 1H NMR spin systems of most amino acid residues of micelle-bound melittin identified. One- and two-dimensional 1H-1H Overhauser experiments have now been used to obtain qualitative information on intramolecular proton-proton distances. These data show that the N-terminal and the C-terminal segments of melittin form two spatially distinct, compact domains; using lipid spin labels these could be located near the micelle surface. For the C-terminal domain a detailed conformation was determined by using the distance contraints from the Overhauser studies as input for a distance geometry algorithm.

subject areas

  • Animals
  • Bee Venoms
  • Bees
  • Electron Spin Resonance Spectroscopy
  • Magnetic Resonance Spectroscopy
  • Melitten
  • Micelles
  • Models, Molecular
  • Phosphorylcholine
  • Protein Conformation
  • Spin Labels
scroll to property group menus

Identity

PubMed Central ID

  • PMC1329145

International Standard Serial Number (ISSN)

  • 0006-3495

Digital Object Identifier (DOI)

  • 10.1016/S0006-3495(82)84680-8

PubMed ID

  • 6275926
scroll to property group menus

Additional Document Info

start page

  • 319

end page

  • 328

volume

  • 37

issue

  • 1

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support