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Backbone 1H, 13C and 15N resonance assignments of an intrinsically unstructured βγ-crystallin from Hahella chejuensis

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Abstract

The sequence specific backbone 1H, 13C and 15N 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 Ca2+-bound structured protein.

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Acknowledgement

The facilities provided by the National Facility for High Field NMR, supported by the Department of Science and Technology (DST), Department of Biotechnology (DBT), Council of Scientific and Industrial Research (CSIR), and Tata Institute of Fundamental Research (TIFR), Mumbai, are gratefully acknowledged.

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Authors and Affiliations

  1. Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai, 400005, India

    Venkatraman Ramanujam, Sunita Patel, Atul K. Srivastava & Kandala V. R. Chary

  2. Center for Cellular and Molecular Biology, Uppal Road, Hyderabad, 500007, India

    Yogendra Sharma

Authors
  1. Venkatraman Ramanujam
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  2. Sunita Patel
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  3. Atul K. Srivastava
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  4. Yogendra Sharma
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  5. Kandala V. R. Chary
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Correspondence to Kandala V. R. Chary.

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Ramanujam, V., Patel, S., Srivastava, A.K. et al. Backbone 1H, 13C and 15N resonance assignments of an intrinsically unstructured βγ-crystallin from Hahella chejuensis . Biomol NMR Assign 7, 221–224 (2013). https://doi.org/10.1007/s12104-012-9414-x

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  • DOI: https://doi.org/10.1007/s12104-012-9414-x

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