D. Sandstrom et al., Identification and mobility of deuterated residues in peptides and proteins by H-2-C-13 solid-state NMR, CHEM P LETT, 300(1-2), 1999, pp. 213-220
We present a solid-state NMR approach for C-13 chemical-shift identificatio
n and H-2 lineshape characterization of amino-acid residues in peptides and
proteins deuterated by amide hydrogen/deuteron exchange. The technique exp
loits heteronuclear C-13-H-2 dipolar couplings to correlate C-13 nuclei and
nearby deuterons. Magic-angle spinning provides high sensitivity and C-13
chemical-site resolution. The simplest version of the experiment, which is
closely related to REDOR, yields a C-13 spectrum permitting identification
of the deuterated residues. in the full two-dimensional experiment, segment
al dynamics are characterized in terms of H-2-NMR lineshapes. The technique
is demonstrated on dipeptides and a 14-kDa protein, with C-13 in natural a
bundance. (C) 1999 Elsevier Science B.V. All rights reserved.