Probing the Interaction between HIV‐1 Protease and the Homodimeric p66/p66’ Reverse Transcriptase Precursor by Double Electron‐Electron Resonance EPR Spectroscopy
Author:
Affiliation:
1. Laboratory of Chemical Physics National Institutes of Diabetes and Digestive and Kidney Diseases National Institutes of Health Building 5, Room B1-30I, 5 Medical Center Drive Bethesda MD 20892–0520 USA
Funder
National Institute of Diabetes and Digestive and Kidney Diseases
Publisher
Wiley
Subject
Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.202000263
Reference37 articles.
1. Retroviral reverse transcriptases
2. Factors affecting the dimerization of the p66 form of HIV-1 reverse transcriptase
3. Proteolytic processing of an HIV-1 pol polyprotein precursor: insights into the mechanism of reverse transcriptase p66/p51 heterodimer formation
4. Structural Maturation of HIV-1 Reverse Transcriptase—A Metamorphic Solution to Genomic Instability
5. Conformational Changes in HIV-1 Reverse Transcriptase that Facilitate Its Maturation
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3. Tm filtering by 1H-methyl labeling in a deuterated protein for pulsed double electron–electron resonance EPR;Chemical Communications;2020
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