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Article

Evolutionary remodeling of βγ-crystallins for domain stability at cost of Ca2+ binding.

The Journal of biological chemistry - 23 Dec 2011

Suman Shashi Kumar, Mishra Amita, Ravindra Daddali, Yeramala Lahari, Sharma Yogendra

Abstract excerpt

The topologically similar βγ-crystallins that are prevalent in all kingdoms of life have evolved for high innate domain stability to perform their specialized functions. The evolution of stability and its control in βγ-crystallins that possess either a canonical (mostly from microorganisms) or degenerate (principally found in vertebrate homologues) Ca2+-binding motif is not known. Using equilibrium unfolding of...

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Identifiers

PMID: 21949186
DOI: 10.1074/jbc.M111.247890
PMCID: PMC3243557

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