Fine tuning the structure of the Cu2+ complex with the prion protein chicken repeat by proline isomerization

Chem Commun (Camb). 2005 Jul 14:(26):3298-300. doi: 10.1039/b504986e. Epub 2005 Jun 1.

Abstract

The interaction between the single hexarepeat unit of chicken prion protein [ChPrP(54-59)] and Cu(II) was investigated by NMR, finding different coordination modes for the trans/trans and cis/trans isomers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Chickens
  • Copper / chemistry*
  • Magnetic Resonance Spectroscopy / methods
  • Models, Molecular
  • Organometallic Compounds / chemistry*
  • Prions / chemistry*
  • Proline / chemistry*
  • Protein Conformation
  • Protein Structure, Tertiary
  • Sensitivity and Specificity
  • Stereoisomerism
  • Structure-Activity Relationship

Substances

  • Organometallic Compounds
  • Prions
  • Copper
  • Proline