Structure of a Cyclic Peptide as an Inhibitor of Mycobacterium tuberculosis Transcription: NMR and Molecular Dynamics Simulations
The NMR-restrained MD simulations showed several low-energy conformations that were congruent with the NMR data. Finally, the conformation of this peptide will be used to design derivatives that can better inhibit RNAP activity.
Authors
- Filia Stephanie (ORCID: https://orcid.org/0000-0002-7861-2045)
- Teruna J. Siahaan (ORCID: https://orcid.org/0000-0001-7250-0627)
- Usman Sumo Friend Tambunan (ORCID: https://orcid.org/0000-0001-6025-2195)
- Krzysztof Kuczera
Institutions
- University of Kansas (US)
- University of Indonesia (ID)
Publication Details
- Journal
- Pharmaceuticals
- Published
- 2024-11-18
- DOI
- https://doi.org/10.3390/ph17111545
- Citations
- 4
- Primary Topic
- Tuberculosis Research and Epidemiology
- Type
- article
- Field-Weighted Citation Impact
- 1.56
Funders
- National Science Foundation
- National Institutes of Health
- National Institute on Aging
- National Institute of General Medical Sciences