Ontology highlight
ABSTRACT:
SUBMITTER: Bonetti D
PROVIDER: S-EPMC4865933 | biostudies-literature | 2016 May
REPOSITORIES: biostudies-literature
Bonetti Daniela D Camilloni Carlo C Visconti Lorenzo L Longhi Sonia S Brunori Maurizio M Vendruscolo Michele M Gianni Stefano S
The Journal of biological chemistry 20160321 20
Although most proteins fold by populating intermediates, the transient nature of such states makes it difficult to characterize their structures. In this work we identified and characterized the structure of an intermediate of the X domain of phosphoprotein (P) of measles virus. We obtained this result by a combination of equilibrium and kinetic measurements and NMR chemical shifts used as structural restraints in replica-averaged metadynamics simulations. The structure of the intermediate was t ...[more]