Insights into the role of hydration in protein structure and stability obtained through hydrostatic pressure studies

AUTOR(ES)

Royer, C.A.

FONTE

Brazilian Journal of Medical and Biological Research

DATA DE PUBLICAÇÃO

2005-08

RESUMO

A thorough understanding of protein structure and stability requires that we elucidate the molecular basis for the effects of both temperature and pressure on protein conformational transitions. While temperature effects are relatively well understood and the change in heat capacity upon unfolding has been reasonably well parameterized, the state of understanding of pressure effects is much less advanced. Ultimately, a quantitative parameterization of the volume changes (at the basis of pressure effects) accompanying protein conformational transitions will be required. The present report introduces a qualitative hypothesis based on available model compound data for the molecular basis of volume change upon protein unfolding and its dependence on temperature.

Documentos Relacionados

• The hydration structure of guanidinium and thiocyanate ions: Implications for protein stability in aqueous solution
• The preaggregated state of an amyloidogenic protein: Hydrostatic pressure converts native transthyretin into the amyloidogenic state
• Stability of Escherichia coli polysomes at high hydrostatic pressure.
• The CATH Database provides insights into protein structure/function relationships.
• Insights into the quaternary association of proteins through structure graphs: a case study of lectins