scholarly journals Chemical shift assignments for Rv0577, a putative glyoxylase associated with virulence from Mycobacterium tuberculosis

2011 ◽  
Vol 6 (1) ◽  
pp. 43-46 ◽  
Author(s):  
Garry W. Buchko ◽  
Heungbok Kim ◽  
Peter J. Myler ◽  
Thomas C. Terwilliger ◽  
Chang-Yub Kim
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Chemical Shift ◽  
Chemical Shift Assignments

scholarly journals Letter to the Editor: 1H, 15N, and 13C chemical shift assignments of the resuscitation promoting factor domain of Rv1009 from Mycobacterium tuberculosis

2004 ◽  
Vol 30 (3) ◽  
pp. 373-374 ◽  
Author(s):  
Martin Cohen-Gonsaud ◽  
Philippe Barthe ◽  
Fran�oise Pommier ◽  
Richard Harris ◽  
Paul C. Driscoll ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Chemical Shift ◽  
Chemical Shift Assignments ◽  
Letter To The Editor ◽  
13C Chemical Shift

Chemical shift assignments of Ribosomal protein S1 from Mycobacterium tuberculosis

2017 ◽  
Vol 11 (2) ◽  
pp. 133-136 ◽  
Author(s):  
Jinglin Fu ◽  
Biling Huang ◽  
Donghai Lin ◽  
Xinli Liao
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Chemical Shift ◽  
Ribosomal Protein ◽  
Chemical Shift Assignments ◽  
Ribosomal Protein S1

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.

Toho-1 β-lactamase: backbone chemical shift assignments and changes in dynamics upon binding with avibactam

2021 ◽  
Author(s):  
Varun V. Sakhrani ◽  
Rittik K. Ghosh ◽  
Eduardo Hilario ◽  
Kevin L. Weiss ◽  
Leighton Coates ◽  
...  
Keyword(s):  
Chemical Shift ◽  
Chemical Shift Assignments ◽  
Backbone Chemical Shift

1H and13C chemical shift assignments of homoisoflavanones

1986 ◽  
Vol 24 (8) ◽  
pp. 663-666 ◽  
Author(s):  
Matteo Adinolfi ◽  
Rosa Lanzetta ◽  
Guglielmo Laonigro ◽  
Michelangelo Parrilli ◽  
Eberhard Breitmaier
Keyword(s):  
Chemical Shift ◽  
Chemical Shift Assignments

scholarly journals 13C and 15N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils

2016 ◽  
Vol 11 (1) ◽  
pp. 75-80 ◽  
Author(s):  
Theint Theint ◽  
Philippe S. Nadaud ◽  
Krystyna Surewicz ◽  
Witold K. Surewicz ◽  
Christopher P. Jaroniec
Keyword(s):  
Chemical Shift ◽  
Prion Protein ◽  
Amyloid Fibrils ◽  
Chemical Shift Assignments
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