Found: 6
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Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150°C
- Published in:
- FEBS Letters, 2006, v. 580, n. 17, p. 4224, doi. 10.1016/j.febslet.2006.06.084
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- Article
Crystal structure of alanyl-tRNA synthetase editing-domain homolog (PH0574) from a hyperthermophile, Pyrococcus horikoshii OT3 at 1.45 Å resolution.
- Published in:
- Proteins, 2006, v. 62, n. 4, p. 1133, doi. 10.1002/prot.20760
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- Article
Crystal structure of the probable haloacid dehalogenase PH0459 from Pyrococcus horikoshii OT3.
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- Protein Science: A Publication of the Protein Society, 2006, v. 15, n. 2, p. 373, doi. 10.1110/ps.051922406
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- Article
Stabilization Mechanism of the Tryptophan Synthase α-Subunit from Thermus thermophilus HB8: X-Ray Crystallographic Analysis and Calorimetry.
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- Journal of Biochemistry, 2005, v. 138, n. 4, p. 343, doi. 10.1093/jb/mvi133
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- Article
Stabilization Due to Dimer Formation of Phosphoribosyl Anthranilate Isomerase from Thermus thermophilus HB8: X-Ray Analysis and DSC Experiments.
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- Journal of Biochemistry, 2005, v. 137, n. 5, p. 569, doi. 10.1093/jb/mvi075
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- Article
Crystal structure of a component of glycine cleavage system: T-protein from Pyrococcus horikoshii OT3 at 1.5 Å resolution.
- Published in:
- Proteins, 2005, v. 58, n. 3, p. 769, doi. 10.1002/prot.20345
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- Article