Hydrogen bond networks determine emergent mechanical and thermodynamic properties across a protein family.

ABSTRACT:

Background

Gram-negative bacteria use periplasmic-binding proteins (bPBP) to transport nutrients through the periplasm. Despite immense diversity within the recognized substrates, all members of the family share a common fold that includes two domains that are separated by a conserved hinge. The hinge allows the protein to cycle between open (apo) and closed (ligated) conformations. Conformational changes within the proteins depend on a complex interplay of mechanical and thermodynamic response, which is manifested as an increase in thermal stability and decrease of flexibility upon ligand binding.

Results

We use a distance constraint model (DCM) to quantify the give and take between thermodynamic stability and mechanical flexibility across the bPBP family. Quantitative stab

SUBMITTER: Livesay DR 

PROVIDER: S-EPMC2533333 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature