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Korchuganov DS Gagnidze IE Tkach EN Schulga AA Kirpichnikov MP Arseniev AS 《Journal of biomolecular NMR》2004,30(4):431-442
An accurate determination of the overall rotation of a protein plays a crucial role in the investigation of its internal motions by NMR. In the present work, an innovative approach to the determination of the protein rotational correlation time R from the heteronuclear relaxation data is proposed. The approach is based on a joint fit of relaxation data acquired at several viscosities of a protein solution. The method has been tested on computer simulated relaxation data as compared to the traditional R determination method from T1/T2 ratio. The approach has been applied to ribonuclease barnase from Bacillus amyloliquefaciens dissolved in an aqueous solution and deuterated glycerol as a viscous component. The resulting rotational correlation time of 5.56 ± 0.01 ns and other rotational diffusion tensor parameters are in good agreement with those determined from T1/T2 ratio. 相似文献
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Korchuganov DS Shul'ga AA Ermoliuk IaS Mit'kevich VA Reĭbarkh MIa Nol'de SB Makarov AA Arsen'ev AS Kirpichnikov MP 《Bioorganicheskaia khimiia》2004,30(6):638-643
The C40,82A;I87E mutant of barstar, an intracellular inhibitor of the ribonuclease barnase from Bacillus amyloliquefaciens, was obtained, and its physicochemical properties were studied. It was produced as a fusion protein with thioredoxin and then cleaved from this by EKmax enterokinase. The mutant was shown by NMR to retain the spatial structure of the wild-type protein but, in contrast to barstar, does not form the homodimers characteristic of barstar in aqueous solution. The mutant protein binds barnase with the dissociation constant (6.6 +/- 1.1) x 10(-11) M and exhibits other physicochemical properties similar to those of the wild-type barstar. This allows the use of C40,82A;I87E mutant instead of wild-type barstar in investigations where the protein dimerization is undesirable. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2004, vol. 30, no. 6; see also http://www.maik.ru. 相似文献
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Korchuganov D. S. Schulga A. A. Ermolyuk Ya. S. Mitkevich V. A. Reibarkh M. Ya. Nolde S. B. Makarov A. A. Arseniev A. S. Kirpichnikov M. P. 《Russian Journal of Bioorganic Chemistry》2004,30(6):577-581
The C40,82A;I87E mutant of barstar, an intracellular inhibitor of the ribonuclease barnase from Bacillus amyloliquefaciens, was obtained, and its physicochemical properties were studied. It was produced as a fusion protein with thioredoxin and then cleaved from this by EKmax enterokinase. The mutant was shown by NMR to retain the spatial structure of the wild-type protein but, in contrast to barstar, does not form the homodimers characteristic of barstar in aqueous solution. The mutant protein binds barnase with the dissociation constant (6.6 ± 1.1) × 10–11 M and exhibits other physicochemical properties similar to those of the wild-type barstar. This allows the use of C40,82A;I87E mutant instead of wild-type barstar in the investigations where the protein dimerization is undesirable. 相似文献
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