Ontology highlight
ABSTRACT:
SUBMITTER: Frueh DP
PROVIDER: S-EPMC2749991 | biostudies-literature | 2009 Sep
REPOSITORIES: biostudies-literature
Frueh Dominique P DP Arthanari Haribabu H Koglin Alexander A Walsh Christopher T CT Wagner Gerhard G
Journal of the American Chemical Society 20090901 36
We present an experiment that allows for a straightforward assignment of NMR resonances, even in large and/or challenging proteins. A single 3D double-TROSY experiment provides three pairs of sequential correlations between two alpha carbons, two amide protons, and two nitrogen nuclei. Thus, all correlated nuclei can readily be visualized within all dimensions of the resulting spectrum, and chain elongation of sequential amino acids can be effected with this single data set. This resolves ambigu ...[more]