Related Experiment Video
Updated: Jun 26, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
4D 1H-13C NMR spectroscopy for assignments of alanine methyls in large and complex protein structures
Devon Sheppard1, Chenyun Guo, Vitali Tugarinov
1Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA.
Abstract:
Alanine (13)CH(3) methyl groups can serve as a useful addition to the Ile, Leu, Val (ILV) selective isotope labeling methodology adopted for NMR studies of high-molecular-weight protein systems. A four-dimensional (4D) methyl-detected "out-and-back" NMR experiment has been developed that allowed us to obtain practically complete (1)H-(13)C assignments of more than 70 alanine methyl sites in a 723-residue enzyme Malate Synthase G. It can be anticipated that the developed NMR methodology will promote the use of alanine methyls as important probes of molecular structure and dynamics in large proteins.
Related Concept Videos
NMR Spectroscopy Of Amines
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
NMR Spectroscopy and Mass Spectrometry of Aldehydes and Ketones
¹H NMR: Complex Splitting
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied first.
¹H NMR of Labile Protons: Deuterium (²H) Substitution

