βB1-Crystallin: Thermodynamic Profiles of Molecular Interactions

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βB1-Crystallin: Thermodynamic Profiles of Molecular Interactions

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 tetr...

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The cis-elements responsible for the high-level, lens-specific expression of the chicken beta B1-crystallin gene were investigated by generating mice harboring beta B1-crystallin promoter/chloramphenicol acetyl transferase (CAT) transgenes. Deletion of promoter sequences -434/-153 and -152/-127 as well as site-directed mutagenesis of the PL1 (-116/-102) and Pl2 (-90/-76) elements significantly ...

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Analysis of crystallin-crystallin interactions by surface plasmon resonance.

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ژورنال

عنوان ژورنال: PLoS ONE

سال: 2012

ISSN: 1932-6203

DOI: 10.1371/journal.pone.0029227