Ontology highlight
ABSTRACT:
SUBMITTER: Poulsen H
PROVIDER: S-EPMC3346126 | biostudies-literature | 2012 May
REPOSITORIES: biostudies-literature
Poulsen Hanne H Nissen Poul P Mouritsen Ole G OG Khandelia Himanshu H
The Journal of biological chemistry 20120320 19
Phosphorylation is one of the major mechanisms for posttranscriptional modification of proteins. The addition of a compact, negatively charged moiety to a protein can significantly change its function and localization by affecting its structure and interaction network. We have used all-atom Molecular Dynamics simulations to investigate the structural consequences of phosphorylating the Na(+)/K(+)-ATPase (NKA) residue Ser(936), which is the best characterized phosphorylation site in NKA, targeted ...[more]