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Zhang H, Hou G, Lu M, et al. HIV-1 Capsid Function Is Regulated by Dynamics: Quantitative Atomic-Resolution Insights by Integrating Magic-Angle-Spinning NMR, QM/MM, and MD. J Am Chem Soc. 2016;138(42):14066-14075doi: 10.1021/jacs.6b08744.
Zhang, H., Hou, G., Lu, M., Ahn, J., Byeon, I. L., Langmead, C. J., Perilla, J. R., Hung, I., Gor'kov, P. L., Gan, Z., Brey, W. W., Case, D. A., Schulten, K., Gronenborn, A. M., & Polenova, T. (2016). HIV-1 Capsid Function Is Regulated by Dynamics: Quantitative Atomic-Resolution Insights by Integrating Magic-Angle-Spinning NMR, QM/MM, and MD. Journal of the American Chemical Society, 138(42), 14066-14075. https://doi.org/10.1021/jacs.6b08744
Zhang, Huilan, et al. "HIV-1 Capsid Function Is Regulated by Dynamics: Quantitative Atomic-Resolution Insights by Integrating Magic-Angle-Spinning NMR, QM/MM, and MD." Journal of the American Chemical Society vol. 138,42 (2016): 14066-14075. doi: https://doi.org/10.1021/jacs.6b08744
Zhang H, Hou G, Lu M, Ahn J, Byeon IL, Langmead CJ, Perilla JR, Hung I, Gor'kov PL, Gan Z, Brey WW, Case DA, Schulten K, Gronenborn AM, Polenova T. HIV-1 Capsid Function Is Regulated by Dynamics: Quantitative Atomic-Resolution Insights by Integrating Magic-Angle-Spinning NMR, QM/MM, and MD. J Am Chem Soc. 2016 Oct 26;138(42):14066-14075. doi: 10.1021/jacs.6b08744. Epub 2016 Oct 18. PMID: 27701859; PMCID: PMC5380593.
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J Am Chem Soc. 2016 Oct 26;138(42):14066-14075. doi: 10.1021/jacs.6b08744. Epub 2016 Oct 18.

HIV-1 Capsid Function Is Regulated by Dynamics: Quantitative Atomic-Resolution Insights by Integrating Magic-Angle-Spinning NMR, QM/MM, and MD.

Journal of the American Chemical Society

Huilan Zhang, Guangjin Hou, Manman Lu, Jinwoo Ahn, In-Ja L Byeon, Christopher J Langmead, Juan R Perilla, Ivan Hung, Peter L Gor'kov, Zhehong Gan, William W Brey, David A Case, Klaus Schulten, Angela M Gronenborn, Tatyana Polenova

Affiliations

  1. Department of Chemistry and Biochemistry, University of Delaware , Newark, Delaware 19716, United States.
  2. Pittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine , 1051 Biomedical Science Tower 3, 3501 Fifth Avenue, Pittsburgh, Pennsylvania 15261, United States.
  3. Department of Structural Biology, University of Pittsburgh School of Medicine , 3501 Fifth Avenue, Pittsburgh, Pennsylvania 15261, United States.
  4. Computer Science Department, Carnegie Mellon University , Gates Hillman Center, 5000 Forbes Avenue, Pittsburgh, Pennsylvania 15213, United States.
  5. Department of Physics and Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.
  6. National High Magnetic Field Laboratory, Florida State University , Tallahassee, Florida 32310, United States.
  7. Department of Chemistry and Chemical Biology, Rutgers University , 174 Frelinghuysen Road, Piscataway, New Jersey 08854-8087, United States.

PMID: 27701859 PMCID: PMC5380593 DOI: 10.1021/jacs.6b08744

Abstract

HIV-1 CA capsid protein possesses intrinsic conformational flexibility, which is essential for its assembly into conical capsids and interactions with host factors. CA is dynamic in the assembled capsid, and residues in functionally important regions of the protein undergo motions spanning many decades of time scales. Chemical shift anisotropy (CSA) tensors, recorded in magic-angle-spinning NMR experiments, provide direct residue-specific probes of motions on nano- to microsecond time scales. We combined NMR, MD, and density-functional-theory calculations, to gain quantitative understanding of internal backbone dynamics in CA assemblies, and we found that the dynamically averaged

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