Ontology highlight
ABSTRACT:
SUBMITTER: Vincent SJ
PROVIDER: S-EPMC20731 | biostudies-literature | 1997 Apr
REPOSITORIES: biostudies-literature
Vincent S J SJ Zwahlen C C Post C B CB Burgner J W JW Bodenhausen G G
Proceedings of the National Academy of Sciences of the United States of America 19970401 9
We have reinvestigated the conformation of NAD+ bound to dogfish lactate dehydrogenase (LDH) by using an NMR experiment that allows one to exploit nuclear Overhauser effects to determine internuclear distances between pairs of protons, without perturbation of spin-diffusion effects from other protons belonging either to the cofactor or to the binding pocket of the enzyme. The analysis indicates that the structure of bound NAD+ is in accord with the conformation determined in the solid state by x ...[more]