NMR of fd coat protein

Journal of Supramolecular Structure
T A Cross, S J Opella

Abstract

The conformations of the major coat protein of a filamentous bacteriophage can be described by nuclear magnetic resonance spectroscopy of the protein and the virus. The NMR experiments involve detection of the 13C and 1H nuclei of the coat protein. Both the 13C and 1H nuclear magnetic resonance (NMR) spectra show that regions of the polypeptide chain have substantially more motion than a typical globular protein. The fd coat protein was purified by gel chromatography of the SDA solubilized virus. Natural abundance 13C NMR spectra at 38 MHz resolve all of the nonprotonated aromatic carbons from the three phenylalanines, two tyrosines, and one tryptophan of the coat protein. The alpha carbons of the coat protein show at least two different classes of relaxation behavior, indicative of substantial variation in the motion of the backbone carbons in contrast to the rigidity of the alpha carbons of globular proteins. The 1H spectrum at 360 MHz shows all of the aromatic carbons and many of the amide protons. Titration of a 1H spectra gives the pKas for the tyrosines.

References

Apr 13, 2013·Annual Review of Analytical Chemistry·S J Opella
Mar 4, 2014·Progress in Biophysics and Molecular Biology·D A MarvinS K Straus
Jul 18, 2014·Quarterly Reviews of Biophysics·Jasmina RadoicicS J Opella
Feb 10, 1987·Biochemistry·G C LeoS J Opella
Mar 19, 2014·Soft Matter·Kyongok Kang

Citations

Dec 1, 1975·Proceedings of the National Academy of Sciences of the United States of America·W T Wickner
Mar 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·K ItoW T Wickner
Feb 1, 1976·The British Journal of Ophthalmology·U W Wüthrich
Sep 25, 1974·Journal of Molecular Biology·Y Nakashima, W Konigsberg
Oct 30, 1974·Journal of the American Chemical Society·S J OpellaO Jardetzyk

Related Concepts

In Vivo NMR Spectroscopy
Viral Proteins
Protein Conformation
Coliphages
Hydrogen-Ion Concentration
GOLPH3

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