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High-resolution h-1-NMR studies of monomeric melittin in aqueous-solution

Academic Article
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Overview

authors

  • Lauterwein, J.
  • Brown, L. R.
  • Wuthrich, Kurt

publication date

  • 1980

journal

  • Biochimica et Biophysica Acta  Journal

abstract

  • High resolution 1H-NMR at 360 MHz was used to characterize monomeric melittin in aqueous solution. The monomeric form of melittin was found to prevail at 3 mM concentration, pH 3.0, and temperatures between 30 and 90 degrees C, both in the absence of salt and with 6 M guanidium chloride. From comparison with model peptides and studies of the effects of 6 M guanidium chloride and variable temperature on the NMR parameters it was concluded that monomeric melittin is predominantly in an extended flexible form, with the fragments 5--9 and 14--20 more highly structured than the rest of the amino acid sequence. The appearance of a second, low abundant form of monomeric melittin, which is in slow exchange on the NMR time scale with both the more abundant monomeric conformation and aggregated melittin, was attributed to cis-trans isomerism of the peptide bond Leu-13--Pro-14.

subject areas

  • Amino Acid Sequence
  • Animals
  • Bee Venoms
  • Bees
  • Guanidine
  • Guanidines
  • Magnetic Resonance Spectroscopy
  • Melitten
  • Micelles
  • Molecular Conformation
  • Solutions
  • Stereoisomerism
  • Temperature
  • Water
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Identity

International Standard Serial Number (ISSN)

  • 0006-3002

Digital Object Identifier (DOI)

  • 10.1016/0005-2795(80)90033-1

PubMed ID

  • 7378451
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Additional Document Info

start page

  • 219

end page

  • 230

volume

  • 622

issue

  • 2

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