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KMID : 0578320070240030437
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Molecules and Cells
2007 Volume.24 No. 3 p.437 ~ p.440
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Backbone 1H, 15N, and 13C Resonance Assignments and Secondary Structure of a Novel Protein OGL-20PT-358 from Hyperthermophile Thermococcus thioreducens sp. nov.
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Wilson Randall C.
Hughes Ronny C.
Curto Ernest V.
NG Joseph D.
Twigg Pamela D.
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Abstract
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OGL-20PT-358 is a novel 66 amino acid residue protein from the hyperthermophile Thermococcus thioreducens sp. nov., strain OGL-20PT, which was collected from the wall of the hydrothermal black smoker in the Rainbow Vent along the mid-Atlantic ridge. This protein, which has no detectable sequence homology with proteins or domains of known function, has a calculated pI of 4.76 and a molecular mass of 8.2 kDa. We report here the backbone 1H, 15N, and 13C resonance assignments of OGL-20PT-358. Assignments are 97.5% (316/324) complete. Chemical shift index was used to determine the secondary structure of the protein, which appears to consist of primarily ?-helical regions. This work is the foundation for future studies to determine the three-dimensional solution structure of the protein.
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KEYWORD
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Backbone Resonance Assignment, Hypothetical Protein, NMR, OGL-20PT-358, Thermococcus Thioreducens, Thermophiles
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