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Your search keyword '"Cowieson, Nathan"' showing total 8 results
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8 results on '"Cowieson, Nathan"'

1. Controlling Photocatalytic Activity by Self‐Assembly – Tuning Perylene Bisimide Photocatalysts for the Hydrogen Evolution Reaction

Author

McDowall, Daniel, primary, Greeves, Benjamin J., additional, Clowes, Rob, additional, McAulay, Kate, additional, Fuentes‐Caparrós, Ana M., additional, Thomson, Lisa, additional, Khunti, Nikul, additional, Cowieson, Nathan, additional, Nolan, Michael C., additional, Wallace, Matthew, additional, Cooper, Andrew I., additional, Draper, Emily R., additional, Cowan, Alexander J., additional, and Adams, Dave J., additional

Published
2020
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8. Assembly and solution structure of the core retromer protein complex.

Author

Norwood SJ, Shaw DJ, Cowieson NP, Owen DJ, Teasdale RD, and Collins BM

Subjects
Amino Acid Motifs, Amino Acid Sequence, Calorimetry, Conserved Sequence, Crystallography, X-Ray, Humans, Molecular Sequence Data, Quantum Theory, Solutions chemistry, Vesicular Transport Proteins chemistry, Models, Molecular, Multiprotein Complexes chemistry
Abstract

Retromer is a peripheral membrane protein complex that has pleiotropic roles in endosomal membrane trafficking. The core of retromer possesses three subunits, VPS35, VPS29 and VPS26, that play different roles in binding to cargo, regulatory proteins and complex stabilization. We have performed an investigation of the thermodynamics of core retromer assembly using isothermal titration calorimetry (ITC) demonstrating that VPS35 acts as the central subunit to which VPS29 and VPS26 bind independently. Furthermore, we confirm that the conserved PRLYL motif of the large VPS35 subunit is critical for direct VPS26 interaction. Heat capacity measurements of VPS29 and VPS26 binding to VPS35 indicate extensive binding interfaces and suggest conformational alterations in VPS29 or VPS35 upon complex formation. Solution studies of the retromer core using small-angle X-ray scattering allow us to propose a model whereby VPS35 forms an extended platform with VPS29 and VPS26 bound at distal ends, with the potential for forming dimeric assemblies., (© 2010 John Wiley & Sons A/S.)

Published
2011
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