Backbone and side-chain chemical shift assignments for the C-terminal domain of Tcb2, a cytoskeletal calcium-binding protein from Tetrahymena thermophila

2016 ◽  
Vol 10 (2) ◽  
pp. 281-285
Author(s):  
Adina M. Kilpatrick ◽  
Theodore E. Gurrola ◽  
Robert C. Sterner ◽  
Heidi M. Sleister ◽  
Jerry E. Honts ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Calcium Binding ◽  
Tetrahymena Thermophila ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Side Chain ◽  
Chemical Shift Assignments ◽  
Terminal Domain ◽  
Side Chain Chemical Shift

1H, 13C, and 15N chemical shift assignments of neuronal calcium sensor-1, a multi-functional calcium-binding protein

2006 ◽  
Vol 36 (S1) ◽  
pp. 48-48 ◽  
Author(s):  
Sulakshana Mukherjee ◽  
Dasari Muralidhar ◽  
Hanudatta S. Atreya ◽  
Thomas Szyperski ◽  
Andreas Jeromin ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Calcium Sensor ◽  
Chemical Shift Assignments ◽  
Neuronal Calcium Sensor

scholarly journals Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered

2021 ◽  
Vol 15 (2) ◽  
pp. 441-448
Author(s):  
Christoph Wiedemann ◽  
Kingsley Benjamin Obika ◽  
Sandra Liebscher ◽  
Jan Jirschitzka ◽  
Oliver Ohlenschlãger ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Intrinsically Disordered Protein ◽  
Genome Project ◽  
Side Chain ◽  
Resonance Spectroscopy ◽  
Chemical Shift Assignments ◽  
Uncharacterized Protein ◽  
Protein Coding ◽  
Intrinsically Disordered ◽  
Side Chain Chemical Shift

AbstractEven though the human genome project showed that our DNA contains a mere 20,000 to 25,000 protein coding genes, an unexpectedly large number of these proteins remain functionally uncharacterized. A structural characterization of these “unknown” proteins may help to identify possible cellular tasks. We therefore used a combination of bioinformatics and nuclear magnetic resonance spectroscopy to structurally de-orphanize one of these gene products, the 108 amino acid human uncharacterized protein CXorf51A. Both our bioinformatics analysis as well as the $$^1$$ 1 H, $$^{13}$$ 13 C, $$^{15}$$ 15 N backbone and near-complete side-chain chemical shift assignments indicate that it is an intrinsically disordered protein.

1H, 13C, and 15N backbone and side-chain chemical shift assignments for the 31 kDa human galectin-7 (p53-induced gene 1) homodimer, a pro-apoptotic lectin

2011 ◽  
Vol 6 (2) ◽  
pp. 127-129 ◽  
Author(s):  
Irina V. Nesmelova ◽  
Manuel Álvaro Berbís ◽  
Michelle C. Miller ◽  
F. Javier Cañada ◽  
Sabine André ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Side Chain ◽  
Chemical Shift Assignments ◽  
Side Chain Chemical Shift
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