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Updated: Aug 11, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
NMR studies and semi-empirical energy calculations for cyclic ADP-ribose
T J Rutherford1, J Wilkie, C Q Vu
1School of Chemistry, University of Birmingham, Edgbaston, UK. t.j.rutherford@bham.ac.uk
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.
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