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Updated: Jul 18, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Locating hydrogen atoms in single crystal and uniaxially aligned amino acids by solid-state NMR
Benjamin J Gross1, Ann E McDermott
1Department of Chemistry, Columbia University, New York, NY 10027, USA. bjg30@columbia.edu
Abstract:
We demonstrate a novel method to locate hydrogen atoms in amino acids, which involves measuring the C(alpha)H(alpha) bond vector geometry through orientationally dependent dipolar coupling frequencies measured by Lee-Goldburg cross polarization (LGCP). A 2D LGCP experiment is used to measure the polar angle of the C(alpha)H(alpha) bond vector in a single crystal of the model compound L-alanine. It is also demonstrated that by coupling the 13C(alpha)1H(alpha) LGCP experiment to a 13C(alpha)15N REDOR experiment, one can determine the complete three-dimensional geometry of the C(alpha)H(alpha) and C(alpha)N vectors in a single crystal. These measurements allow for location of hydrogen atoms in crystalline biological macromolecules.
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