Robert M. J. Jacobs
University of Oxford
70 Papers
841 Citations
Robert M. J. Jacobs is an academic researcher from University of Oxford. The author has contributed to research in topics: Chemistry & Globular protein. The author has an hindex of 33, co-authored 70 publications. Previous affiliations of Robert M. J. Jacobs include Mansfield University of Pennsylvania & European Synchrotron Radiation Facility.
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Papers
Protein interactions studied by SAXS: effect of ionic strength and protein concentration for BSA in aqueous solutions.
Fajun Zhang,Maximilian W. A. Skoda,Robert M. J. Jacobs,Richard Martin,Christopher M. Martin,Frank Schreiber +5 more
TL;DR: Although the long-range, attractive potential dominated the protein interaction, no gelation or precipitation was observed in any of the samples, and the fit parameters indicate that the attractive potential caused by a high salt concentration is weak and long-ranged.
305
Reentrant Condensation of Proteins in Solution Induced by Multivalent Counterions
Fan Zhang,Maximilian W. A. Skoda,Maximilian W. A. Skoda,Robert M. J. Jacobs,Stefan Zorn,Richard Martin,Christopher M. Martin,Graham F. Clark,S. Weggler,Andreas Hildebrandt,Oliver Kohlbacher,Frank Schreiber +11 more
TL;DR: Monte Carlo simulations (under these strong electrostatic coupling conditions) support an effective inversion of charge on surface side chains through binding of the multivalent counterions.
231
TOF-2: a large 1D channel thorium organic framework.
TL;DR: A new neutral 1D channel thorium organic framework material (TOF-2) has been synthesized under hydrothermal conditions and gas adsorption measurements show deferential gas uptake behavior.
137
Universality of protein reentrant condensation in solution induced by multivalent metal ions.
Fajun Zhang,Sophie Weggler,Michael J. Ziller,Luca Ianeselli,Benjamin S. Heck,Andreas Hildebrandt,Oliver Kohlbacher,Maximilian W. A. Skoda,Robert M. J. Jacobs,Frank Schreiber +9 more
TL;DR: The question of universality of the reentrant condensation of proteins in solution induced by multivalent counterions is discussed, i.e., redissolution on adding further salts after phase separation, as recently discovered.
129
Protein-protein interactions in ovalbumin solutions studied by small-angle scattering: effect of ionic strength and the chemical nature of cations.
Luca Ianeselli,Fajun Zhang,Maximilian W. A. Skoda,Robert M. J. Jacobs,Richard Martin,Shirley Callow,Sylvain Prévost,Frank Schreiber +7 more
TL;DR: The influence of ionic strength and of the chemical nature of cations on the protein-protein interactions in ovalbumin solution was studied using small-angle X-ray and neutron scattering (SAXS/SANS).