Search

Your search keyword '"Yalloway, Gary N."' showing total 7 results
Start Over Author "Yalloway, Gary N." Search Limiters Full Text
7 results on '"Yalloway, Gary N."'

1. Simultaneous sequencing of genetic and epigenetic bases in DNA

Author

Füllgrabe, Jens, Gosal, Walraj S., Creed, Páidí, Liu, Sidong, Lumby, Casper K., Morley, David J., Ost, Tobias W. B., Vilella, Albert J., Yu, Shirong, Bignell, Helen, Burns, Philippa, Charlesworth, Tom, Fu, Beiyuan, Fordham, Howerd, Harding, Nicolas J., Gandelman, Olga, Golder, Paula, Hodson, Christopher, Li, Mengjie, Lila, Marjana, Liu, Yang, Mason, Joanne, Mellad, Jason, Monahan, Jack M., Nentwich, Oliver, Palmer, Alexandra, Steward, Michael, Taipale, Minna, Vandomme, Audrey, San-Bento, Rita Santo, Singhal, Ankita, Vivian, Julia, Wójtowicz, Natalia, Williams, Nathan, Walker, Nicolas J., Wong, Nicola C. H., Yalloway, Gary N., Holbrook, Joanna D., and Balasubramanian, Shankar

Published
2023
Full Text
View/download PDF

5. Simultaneous measurement of protein one-bond and two-bond nitrogen-carbon coupling constants using an internally referenced quantitative J-correlated [15N,1H]-TROSY-HNC experiment.

Author

Wienk, Hans L.J., Martínez, Mitcheell M., Yalloway, Gary N., Schmidt, Jürgen M., Pérez, Carlos, Rüterjans, Heinz, and Löhr, Frank

Subjects
PROTEINS, BIOMOLECULES, CARBON, ELASTIC solids, PROTON transfer reactions
Abstract

A quantitative J-correlation pulse sequence is described that allows simultaneous determination of one-bond and two-bond nitrogen-carbon coupling constants for protonated or deuterated proteins. Coupling constants are calculated from volume ratios between cross peaks and reference axial peaks observed in a single 3D spectrum. Accurate backbone 1JNC′, 1JNCα, and 2JNCα coupling constants are obtained for the two [15N;13C]-labeled, medium-sized proteins flavodoxin and xylanase and for the [2H;15N;13C]-labeled, large protein DFPase. A dependence of one-bond and two-bond JNCα values on protein backbone ψ torsion angles is readily apparent, in agreement with previously found correlations. In addition, the experiment is performed on isotropic as well as aligned protein to measure associated 15N-13C residual dipolar couplings. [ABSTRACT FROM AUTHOR]

Published
2003
Full Text
View/download PDF

6. Letter to the Editor: 1H, 13C and 15N assignment of the hydroquinone form of flavodoxin from Desulfovibrio vulgaris (Hildenborough) and comparison of the chemical shift differences with respect to the oxidized state.

Author

Yalloway, Gary N., Löhr, Frank, Wienk, Hans L., Mayhew, Stephen G., Hrovat, Andrea, Knauf, Martin A., and Rüterjans, Heinz

Subjects
BACTERIAL proteins, DESULFOVIBRIO, MICROBIAL proteins, HYDROQUINONE, SULFUR bacteria, NUCLEAR magnetic resonance spectroscopy, SPECTRUM analysis, PROTEINS
Abstract

Reports on the complete assignment of the chemical shifts for the hydroquinone of Desulfovibrio vulgaris wild-type flavodoxin and the deposition of the chemical shifts for the oxidized and fully reduced states. Comparison of the chemical shift differences between these two redox states; Extent of assignment and data deposition.

Published
2003
Full Text
View/download PDF

7. 1H, 13C and 15N assignment of the hydroquinone form of flavodoxin from Desulfovibrio vulgaris (Hildenborough) and comparison of the chemical shift differences with respect to the oxidized state.

Author

Yalloway GN, Löhr F, Wienk HL, Mayhew SG, Hrovat A, Knauf MA, and Rüterjans H

Subjects
Carbon Isotopes chemistry, Databases as Topic, Hydrogen chemistry, Hydrogen Bonding, Models, Chemical, Nitrogen Isotopes chemistry, Oxidation-Reduction, Protein Conformation, Protein Structure, Secondary, Protons, Desulfovibrio vulgaris metabolism, Flavodoxin chemistry, Hydroquinones chemistry, Magnetic Resonance Spectroscopy methods, Oxygen metabolism
Published
2003
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results