ИСТИНА |
Войти в систему Регистрация |
|
ИСТИНА ИНХС РАН |
||
Studies of molecular recognition processes demand much high accuracy of determination of protein structure than it achieved with the standard techniques of NMR spectroscopy. Research carried out during the reporting period was focused on developing of new methods and application of recently invented techniques aimed at obtaining high accuracy and precision of protein structure in solution. Long-range global constraints based on residual dipolar couplings were used to refine NMR structure of ternary complex of Lactobacillus casei with NADPH and trimethoprim. Combination of experimental NMR data and ab inito quantum mechanical calculations was used to determine the nature of specificity of binding the reduced and oxidized forms of nicotinamide adenine dinucleotide phosphate coenzyme to dihydrofolate reductase.