James Gowdy
University of Leeds
5 Papers
35 Citations
James Gowdy is an academic researcher from University of Leeds. The author has contributed to research in topics: Glucose transporter & Small molecule. The author has an hindex of 4, co-authored 5 publications.
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Papers
Nonexponential Kinetics of Loop Formation in Proteins and Peptides: A Signature of Rugged Free Energy Landscapes?
TL;DR: This work presents simulations, with different atomistic models, of short peptides with varied structural propensity, and of a structured protein, showing exponential contact formation kinetics at long times, and a power law relaxation at very short times.
Revealing low-dose radiation damage using single-crystal spectroscopy
TL;DR: Data on the rapid reduction of haem proteins in the X-ray beam at synchrotron sources and the use of single-crystal spectroscopy to detect these changes and their implication for diffraction data collection from oxidized species are presented.
TROSY NMR with a 52 kDa sugar transport protein and the binding of a small-molecule inhibitor.
Arnout P. Kalverda,James Gowdy,Gary S. Thompson,Steve W. Homans,Peter J. F. Henderson,Simon G. Patching +5 more
TL;DR: It is demonstrated that high-resolution TROSY NMR spectra can be achieved with large complex α-helical membrane proteins without the use of elevated temperatures and is a prerequisite to applying further labelling strategies and NMR experiments for measurement of dynamics, structure elucidation and use of the spectra to screen ligand binding.
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Effect of external pulling forces on the length distribution of peptides.
TL;DR: The utility of constant force to enhance the sampling efficiency and obtain experimentally measurable quantities on a series of short peptides, including charge-rich sequences that are known to be highly helical but whose properties are distinct from those of helical peptides undergoing helix-coil transitions.
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The structure of the PanD/PanZ protein complex reveals negative feedback regulation of pantothenate biosynthesis by coenzyme A.
Diana C. F. Monteiro,Vijay Patel,Christopher Bartlett,Shingo Nozaki,Thomas D. Grant,James Gowdy,Gary S. Thompson,Arnout P. Kalverda,Edward H. Snell,Hironori Niki,Hironori Niki,Arwen R. Pearson,Michael E. Webb +12 more
TL;DR: The structure of PanZ in complex with PanD is reported, which reveals the structural basis for the CoA dependence and shows that PanZ acts as a CoA-dependent inhibitor of ADC catalysis, which represents a previously unobserved mode of metabolic regulation whereby a cofactor-utilizing protein negatively regulates the biosynthesis of the same cofactor.