title: Backbone ¹H, ¹³C and ¹⁵N resonance assignments of an intrinsically unstructured βγ-crystallin from Hahella chejuensis.
abstract: 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.
authors: Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai 400005, India.
authors: Venkatraman
authors: V
authors: Ramanujam
authors: Sunita
authors: S
authors: Patel
authors: Atul K
authors: AK
authors: Srivastava
authors: Yogendra
authors: Y
authors: Sharma
authors: Kandala V R
authors: KV
authors: Chary
mesh_terms: D000595:Amino Acid Sequence; D001059:Apoproteins / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D003459:Crystallins / Q000737:chemistry*; D020563:Gammaproteobacteria / Q000378:metabolism*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011522:Protons
chemical_list: D001059:Apoproteins; D001426:Bacterial Proteins; D002247:Carbon Isotopes; D003459:Crystallins; D009587:Nitrogen Isotopes; D011522:Protons