Figure 1 Internuclear correlations that can be detected on a isotopically labeled protein backbone using the listed triple-resonance experiments. Boxes with a solid outline designate the nuclei involved in each correlation experiment. Dotted vertical lines indicate the location of the peptide bonds.

doi:10.1201/9780203910696-134

Chapter

Figure 1 Internuclear correlations that can be detected on a isotopically labeled protein backbone using the listed triple-resonance experiments. Boxes with a solid outline designate the nuclei involved in each correlation experiment. Dotted vertical lines indicate the location of the peptide bonds.

Chapter

ABSTRACT

NMR allows observation of correlations due to scalar couplings across hydrogen bonds. This indicates that hydrogen bonds can have a measurable amount of covalent character, so the phenomenon has been called “hydrogen-bond J couplings.” Among the correlations observed are one-bond 1hJHN correlations [98], two-bond

2hJNN correlations [99], and three-bond 3hJC’N correlations [100,101], all of which have recently been explained theoretically [102]. Much like a long-range NOE correlation, these correlations add structural constraints to 3D structures (especially for nucleic acids).