Beta-crystallin association

Beta-crystallins are major protein constituents of the mammalian lens, where their stability and association into higher order complexes are critical for lens clarity and refraction. Dimerization is an initial step in formation of beta-crystallin complexes. Beta-crystallin association into dimers is...

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Bibliographic Details
Published in:Experimental eye research 2004-12, Vol.79 (6), p.377-383
Main Authors: Hejtmancik, J F, Wingfield, P T, Sergeev, Y V
Format: Article
Language:English
Subjects:
beta-Crystallin A Chain - metabolism
beta-Crystallin B Chain - metabolism
beta-Crystallins - metabolism
Chromatography, Gel
Hot Temperature
Humans
Isoelectric Focusing
Lens, Crystalline - metabolism
Models, Biological
Ultracentrifugation
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Summary:Beta-crystallins are major protein constituents of the mammalian lens, where their stability and association into higher order complexes are critical for lens clarity and refraction. Dimerization is an initial step in formation of beta-crystallin complexes. Beta-crystallin association into dimers is energetically highly favoured, but rapidly reversible under physiological conditions. Beta-crystallin dimers can exchange monomers, probably through a transient and energetically unfavoured monomer intermediate state. As predicted by molecular modelling, the fraction of beta-Crystallin present as dimers increases with increasing temperature, implying that beta-crystallin association is entropically driven.
ISSN:0014-4835