Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.

ABSTRACT: Many proteins comprising of complex topologies require molecular chaperones to achieve their unique three-dimensional folded structure. The E.coli chaperone, GroEL binds with a large number of unfolded and partially folded proteins, to facilitate proper folding and prevent misfolding and aggregation. Although the major structural components of GroEL are well defined, scaffolds of the non-native substrates that determine chaperone-mediated folding have been difficult to recognize. Here we performed all-atomistic and replica-exchange molecular dynamics simulations to dissect non-native ensemble of an obligate GroEL folder, DapA. Thermodynamics analyses of unfolding simulations revealed populated intermediates with distinct structural characteristics. We found that surface exposed hydrophobic

SUBMITTER: Nagpal S 

PROVIDER: S-EPMC4578939 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature