Abstract:
: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.
journal_name
Exp Eye Resjournal_title
Experimental eye researchauthors
Hejtmancik JF,Wingfield PT,Sergeev YVdoi
10.1016/j.exer.2004.06.011keywords:
subject
Has Abstractpub_date
2004-09-01 00:00:00pages
377-83issue
3eissn
0014-4835issn
1096-0007pii
S0014483504001654journal_volume
79pub_type
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