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Nat Commun. 2019 Mar 4;10(1):1026. doi: 10.1038/s41467-019-08926-3.

Protein and RNA dynamical fingerprinting.

Author information

1
Department of Physics, University at Buffalo, SUNY, Buffalo, NY, USA.
2
National Heart, Lung and Blood Institute, Bethesda, MD, USA.
3
Hauptman-Woodward Medical Research Institute & Department of Structural Biology, University at Buffalo, SUNY, Buffalo, NY, USA.
4
Department of Physics, University of Wisconsin, Milwaukee, WI, USA.
5
Department of Physics, University at Buffalo, SUNY, Buffalo, NY, USA. amarkelz@buffalo.edu.
6
Hauptman-Woodward Medical Research Institute & Department of Structural Biology, University at Buffalo, SUNY, Buffalo, NY, USA. amarkelz@buffalo.edu.

Abstract

Protein structural vibrations impact biology by steering the structure to functional intermediate states; enhancing tunneling events; and optimizing energy transfer. Strong water absorption and a broad continuous vibrational density of states have prevented optical identification of these vibrations. Recently spectroscopic signatures that change with functional state were measured using anisotropic terahertz microscopy. The technique however has complex sample positioning requirements and long measurement times, limiting access for the biomolecular community. Here we demonstrate that a simplified system increases spectroscopic structure to dynamically fingerprint biomacromolecules with a factor of 6 reduction in data acquisition time. Using this technique, polarization varying anisotropy terahertz microscopy, we show sensitivity to inhibitor binding and unique vibrational spectra for several proteins and an RNA G-quadruplex. The technique's sensitivity to anisotropic absorbance and birefringence provides rapid assessment of macromolecular dynamics that impact biology.

PMID:
30833555
PMCID:
PMC6399446
DOI:
10.1038/s41467-019-08926-3
[Indexed for MEDLINE]
Free PMC Article

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