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

被引：1

作者：

Ramanujam, Venkatraman ^{[1
]}

Patel, Sunita ^{[1
]}

Srivastava, Atul K. ^{[1
]}

Sharma, Yogendra ^{[2
]}

Chary, Kandala V. R. ^{[1
]}

机构：

[1] Tata Inst Fundamental Res, Dept Chem Sci, Mumbai 400005, Maharashtra, India

[2] Ctr Cellular & Mol Biol, Hyderabad 500007, Andhra Pradesh, India

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2013年 / 7卷 / 02期

关键词：

Intrinsically unstructured protein; beta gamma-crystallin; Hahella chejuensis; Backbone resonance assignments; AUTOMATED NMR ASSIGNMENTS; CA2+ BINDING; PROTEIN; SUPERFAMILY; CALCIUM; STABILITY; TATAPRO; DOMAINS;

D O I：

10.1007/s12104-012-9414-x

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The sequence specific backbone H-1, C-13 and N-15 resonance assignments of an intrinsically unstructured beta gamma-crystallin from Hahella chejuensis are reported. The secondary structure chracterization of the unstructured protein reveals that large fraction of residues exhibits beta-strand propensity, as in the case of the Ca2+-bound structured protein.

引用

页码：221 / 224

页数：4

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