NMR studies and semi-empirical energy calculations for cyclic ADP-ribose

Nucleosides Nucleotides Nucleic Acids. 2001 Aug;20(8):1485-95. doi: 10.1081/NCN-100105243.

Abstract

A possible pH-dependent conformational switch was investigated for cyclic ADP-ribose. NMR signals for the exchangeable protons were observed in H2O at low temperature, but there was no direct evidence for the protonation of N-3 at neutral pH that has previously been postulated. MNDO calculations indicated that pH dependent 31P chemical shift changes are attributable to protonation of the phosphate adjacent to the N-1 of adenine, and not due to trans-annular hydrogen bonding with a protonated N-3.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Diphosphate Ribose / analogs & derivatives*
  • Adenosine Diphosphate Ribose / chemistry*
  • Cyclic ADP-Ribose
  • Hydrogen Bonding
  • Hydrogen-Ion Concentration
  • Magnetic Resonance Spectroscopy*
  • Models, Molecular
  • Molecular Conformation
  • Protons
  • Thermodynamics

Substances

  • Protons
  • Cyclic ADP-Ribose
  • Adenosine Diphosphate Ribose