Sub-nanoscale surface ruggedness provides a water-tight seal for exposed regions in soluble protein structure.

ABSTRACT: Soluble proteins must maintain backbone hydrogen bonds (BHBs) water-tight to ensure structural integrity. This protection is often achieved by burying the BHBs or wrapping them through intermolecular associations. On the other hand, water has low coordination resilience, with loss of hydrogen-bonding partnerships carrying significant thermodynamic cost. Thus, a core problem in structural biology is whether natural design actually exploits the water coordination stiffness to seal the backbone in regions that are exposed to the solvent. This work explores the molecular design features that make this type of seal operative, focusing on the side-chain arrangements that shield the protein backbone. We show that an efficient sealing is achieved by adapting the sub-nanoscale surface topography to

SUBMITTER: Schulz E 

PROVIDER: S-EPMC2941462 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature