The sequence specific backbone (1)H, (13)C and (15)N resonance assignments of an intrinsically unstructured βγ-crystallin from Hahella chejuensis are reported. The secondary structure chracterization of the unstructured protein reveals that large fraction of residues exhibits β-strand propensity, as in the case of the Ca(2+)-bound structured protein.
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| http://dx.doi.org/10.1007/s12104-012-9414-x | DOI Listing |
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