Structure function insights into elusive Mycobacterium tuberculosis protein Rv1916.

@article{Antil2019StructureFI,
  title={Structure function insights into elusive Mycobacterium tuberculosis protein Rv1916.},
  author={Monika Antil and Jyoti Sharma and Yoan Brissonnet and Monika Choudhary and S{\'e}bastien G. Gouin and Vibha Gupta},
  journal={International journal of biological macromolecules},
  year={2019}
}
Rv1915 and Rv1916 from Mycobacterium tuberculosis H37Rv form in vitro protein-protein complex.
Truncation of C-Terminal Intrinsically Disordered Region of Mycobacterial Rv1915 Facilitates Production of “Difficult-to-Purify” Recombinant Drug Target
TLDR
This study reports optimization of solubilization buffer for recovery of soluble and biologically active recombinant mycobacterial Rv1915/ICL2a from IBs and truncated 90 residues from the C-terminal of Rv 1915/ ICL2 were truncated, supporting the disordered nature of R v19 15/ICl2a C- terminal.
Multi-Omics Approaches to Study Signaling Pathways

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