Ontology highlight
ABSTRACT:
SUBMITTER: Norin M
PROVIDER: S-EPMC1225398 | biostudies-other | 1994 Aug
REPOSITORIES: biostudies-other
Norin M M Haeffner F F Hult K K Edholm O O
Biophysical journal 19940801 2
We report on molecular dynamics simulations of a medium-sized protein, a lipase from Rhizomucor miehei, in vacuum, in water, and in a nonpolar solvent, methyl hexanoate. Depending on force field and solvent, the molecular dynamics structures obtained as averages over 150 ps had root-mean-square deviations in the range of 1.9 to 3.6 A from the crystal structure. The largest differences between the structures were in hydrogen bonding and exposed surface areas of the protein. The surface area incre ...[more]