In Silico analysis of PE_PGRS20 (Rv1068c) protein in Mycobacterium tuberculosis H37Rv

The genetic makeup of Mycobacterium tuberculosis reveals the presence of an unknown repeat sequence of PE_PGRS family proteins that are responsible for antigenic variations and many unknown functions that includes necrosis of macrophage and apoptosis. The structure and function of these glycine-rich proteins can be predictable by homology modeling, the Ab-initio method, or by using different tools of bioinformatics. In this study, we selected, PE_PGRS20 (Rv1068c) an unknown PE_PGRS protein. We suggest that the PE_PGRS20 gene is linked with the others genes of the espACD operon which are the virulence factors in the M. tuberculosis H37Rv strain. The genes associated with this protein secretion system can perform the synthesis of a special type of fatty acid known as phthioceroldimycocerates (PDIM).Docking with different anti TB drugs shows binding with PE_PGRS20 protein which suggests that the target protein may involve in the drug resistance.

Моделирование спектра оптического поглощения межзвездной среды гибридными молекулами C-=SUB=-24-=/SUB=-H-=SUB=-30-=/SUB=-, C-=SUB=-32-=/SUB=-H-=SUB=-36-=/SUB=- и С-=SUB=-73-=/SUB=-Н-=SUB=-74-=/SUB=-

Accounting for the different contributions of the aromatic rings, separated with sp3 bonds, with ab initio method we constructed the hybrid cluster С73Н74 which UV spectrum matches the most noticeable absorption band of 217.5 nm, known from astrophysical observations.