%0 Journal Article
%T ¦ÂB1-Crystallin: Thermodynamic Profiles of Molecular Interactions
%A Monika B. Dolinska
%A Paul T. Wingfield
%A Yuri V. Sergeev
%J PLOS ONE
%D 2012
%I Public Library of Science (PLoS)
%R 10.1371/journal.pone.0029227
%X Background ¦Â-Crystallins are structural proteins maintaining eye lens transparency and opacification. Previous work demonstrated that dimerization of both ¦ÂA3 and ¦ÂB2 crystallins (¦ÂA3 and ¦ÂB2) involves endothermic enthalpy of association (~8 kcal/mol) mediated by hydrophobic interactions. Methodology/Principal Findings Thermodynamic profiles of the associations of dimeric ¦ÂA3 and ¦ÂB1 and tetrameric ¦ÂB1/¦ÂA3 were measured using sedimentation equilibrium. The homo- and heteromolecular associations of ¦ÂB1 crystallin are dominated by exothermic enthalpy (£¿13.3 and £¿24.5 kcal/mol, respectively). Conclusions/Significance Global thermodynamics of ¦ÂB1 interactions suggest a role in the formation of stable protein complexes in the lens via specific van der Waals contacts, hydrogen bonds and salt bridges whereas those ¦Â-crystallins which associate by predominately hydrophobic forces participate in a weaker protein associations.
%U http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0029227