Abstract
Выделение гистидиновой тРНК из Thermus thermophilus и изучение ее первичной структуры и участков взаимодействия с гомологичной аминоацил-тРНК синтетазой
Highlights
The fidelity of protein biosynthesis depends on correct aminoacylation of tRNA by aminoacids
This work describes the isolation of T.thermophilus tRNAHis, the definition of its primary structure and the study of interaction sites with histidyl-tRNA synthetase in the solution
The individual tRNAHis was isolated from crude tRNA, using chromatography on benzoyl-DEAE-cellulose (BD-cellulose), DEAE
Summary
The fidelity of protein biosynthesis depends on correct aminoacylation of tRNA by aminoacids. The crystals of tRNAHis complex with T.thermophilus histidyl-tRNA synthetase were obtained [7], but the structure of this complex was not defined yet. The study of tRNAHis interaction with histidyl-tRNA synthetase in the solution is of significant interest.
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