Ontology highlight
ABSTRACT:
SUBMITTER: Camilloni C
PROVIDER: S-EPMC2492814 | biostudies-literature | 2008 Aug
REPOSITORIES: biostudies-literature
Camilloni Carlo C Sutto Ludovico L Provasi Davide D Tiana Guido G Broglia Ricardo A RA
Protein science : a publication of the Protein Society 20080529 8
The presence of native contacts in the denatured state of many proteins suggests that elements of the biologically active structure of these molecules are formed during the initial stage of the folding process. The rapidity with which these events take place makes it difficult to study them in vitro, but, by the same token, suitable for studies in silico. With the help of all-atom, explicit solvent, molecular dynamics simulations we have followed in time, starting from elongated structureless co ...[more]