19 F Dynamic Nuclear Polarization at Fast Magic Angle Spinning for NMR of HIV-1 Capsid Protein Assemblies
We report remarkably high, up to 100-fold, signal enhancements in F dynamic nuclear polarization (DNP) magic angle spinning (MAS) spectra at 14.1 T on HIV-1 capsid protein (CA) assemblies. These enhancements correspond to absolute sensitivity ratios of 12-29 and are of similar magnitude to those see...
Saved in:
Published in | Journal of the American Chemical Society Vol. 141; no. 14; pp. 5681 - 5691 |
---|---|
Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
10.04.2019
|
Online Access | Get full text |
Cover
Loading…
Summary: | We report remarkably high, up to 100-fold, signal enhancements in
F dynamic nuclear polarization (DNP) magic angle spinning (MAS) spectra at 14.1 T on HIV-1 capsid protein (CA) assemblies. These enhancements correspond to absolute sensitivity ratios of 12-29 and are of similar magnitude to those seen for
H signals in the same samples. At MAS frequencies above 20 kHz, it was possible to record 2D
F-
C HETCOR spectra, which contain long-range intra- and intermolecular correlations. Such correlations provide unique distance restraints, inaccessible in conventional experiments without DNP, for protein structure determination. Furthermore, systematic quantification of the DNP enhancements as a function of biradical concentration, MAS frequency, temperature, and microwave power is reported. Our work establishes the power of DNP-enhanced
F MAS NMR spectroscopy for structural characterization of HIV-1 CA assemblies, and this approach is anticipated to be applicable to a wide range of large biomolecular systems. |
---|---|
ISSN: | 0002-7863 1520-5126 |
DOI: | 10.1021/jacs.8b09216 |