βB1-crystallin: thermodynamic profiles of molecular interactions.

ABSTRACT:

Background

β-Crystallins are structural proteins maintaining eye lens transparency and opacification. Previous work demonstrated that dimerization of both βA3 and βB2 crystallins (βA3 and βB2) involves endothermic enthalpy of association (∼8 kcal/mol) mediated by hydrophobic interactions.

Methodology/principal findings

Thermodynamic profiles of the associations of dimeric βA3 and βB1 and tetrameric βB1/βA3 were measured using sedimentation equilibrium. The homo- and heteromolecular associations of βB1 crystallin are dominated by exothermic enthalpy (-13.3 and -24.5 kcal/mol, respectively).

Conclusions/significance

Global thermodynamics of βB1 interactions suggest a role in the formation of stable protein complexes in the lens via specific van der Waals contacts, hydro

SUBMITTER: Dolinska MB 

PROVIDER: S-EPMC3253074 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature