Structural dynamics of PMP-D2: An experimental and theoretical study

Georges Mer, Annick Dejaegere, Roland Stote, Bruno Kieffer, Jean François Lefèvre

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

PMP-D2 is a 35 residue polypeptide cross-linked by three disulfide bridges. Its three-dimensional structure has been previously determined (Mer et al. Biochemistry 1994, 33, 15397-15407). Further investigation of its structure identified a crucial interaction between W25 and K10 and a double salt bridge between the positively charged K10 and the negatively charged E2 and D13. Chemical shift calculations reveal some discrepancies with experimental data concerning the structure. Heteronuclear relaxation studies, which observed broadening of K10 side chain proton resonances, and molecular dynamics simulations subsequently suggest that these discrepancies are due to slow conformational exchange in the molecule. The heteronuclear relaxation studies and visual inspection of the three-dimensional structure suggest that the residues which exhibit slow exchange form a network and move in a concerted manner.

Original languageEnglish (US)
Pages (from-to)2667-2674
Number of pages8
JournalJournal of physical chemistry
Volume100
Issue number7
StatePublished - Feb 15 1996

    Fingerprint

ASJC Scopus subject areas

  • Engineering(all)
  • Physical and Theoretical Chemistry

Cite this

Mer, G., Dejaegere, A., Stote, R., Kieffer, B., & Lefèvre, J. F. (1996). Structural dynamics of PMP-D2: An experimental and theoretical study. Journal of physical chemistry, 100(7), 2667-2674.