Ontology highlight
ABSTRACT:
SUBMITTER: Kurkcuoglu O
PROVIDER: S-EPMC2556966 | biostudies-literature | 2006 Jan
REPOSITORIES: biostudies-literature
Kurkcuoglu Ozge O Jernigan Robert L RL Doruker Pemra P
Biochemistry 20060101 4
The internal dynamics of triosephosphate isomerase have been investigated with elastic networks, with and without a substrate bound. The slowest modes of motion involve large domain motions but also a loop motion that conforms to the changes observed between the crystal structures and . Our computations confirm that the different motions of this loop are important in several of the computed slowest modes. We have shown that elastic network computations on this protein system can combine atoms fo ...[more]