Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Jordan W. Bye"'
Publikováno v:
ACS Omega, Vol 1, Iss 4, Pp 669-679 (2016)
Externí odkaz:
https://doaj.org/article/b66d13d8313046149de176abd30a754e
Autor:
Cheng Zhang, Jordan W. Bye, Lok H. Lui, Hongyu Zhang, John Hales, Steve Brocchini, Robin A. Curtis, Paul A. Dalby
Publikováno v:
Molecular Pharmaceutics. 20:2650-2661
Publikováno v:
Biomedicines
Volume 9
Issue 11
Biomedicines, Vol 9, Iss 1646, p 1646 (2021)
Bye, J, Murray, K & Curtis, R 2021, ' ATP and tri-polyphosphate (TPP) suppress protein aggregate growth by a supercharging mechanism ', Biomedicines . https://doi.org/10.3390/biomedicines9111646
Volume 9
Issue 11
Biomedicines, Vol 9, Iss 1646, p 1646 (2021)
Bye, J, Murray, K & Curtis, R 2021, ' ATP and tri-polyphosphate (TPP) suppress protein aggregate growth by a supercharging mechanism ', Biomedicines . https://doi.org/10.3390/biomedicines9111646
A common strategy to increase aggregation resistance is through rational mutagenesis to supercharge proteins, which leads to a high colloidal stability, but often has the undesirable effect of lowering conformational stability. We show this trade-off
Autor:
Robin Curtis, Jordan W. Bye
Publikováno v:
Bye, J W & Curtis, R A 2019, ' Controlling Phase Separation of Lysozyme with Polyvalent Anions ', The Journal of Physical Chemistry B, vol. 123, no. 3, pp. 593-605 . https://doi.org/10.1021/acs.jpcb.8b10868
The ability of polyvalent anions to influence protein–protein interactions and protein net charge was investigated through solubility and turbidity experiments, determination of osmotic second virial coefficients (B22), and ζ-potential values for
Autor:
Gregor Herz, James McGregor, Colin L. Freeman, Jordan W. Bye, John D. Howard, Robert J. Falconer
Publikováno v:
Journal of Solution Chemistry
In this paper we demonstrate the application of pressure perturbation calorimetry (PPC) to the characterization of 2-propanol/water mixtures. PPC of different 2-propanol/water mixtures provides two useful measurements: (i) the change in heat (ΔQ); a
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2039
Dynamic light scattering has become a method of choice for measuring and quantifying weak, nonspecific protein-protein interactions due to its ease of use, minimal sample consumption, and amenability to high-throughput screening via plate readers. A
Autor:
Jordan W. Bye, Robert J. Falconer
Publikováno v:
The Journal of Physical Chemistry B. 118:4282-4286
Addition of high and medium charge density anions (phosphate, sulfate, and chloride) to lysozyme in pure water demonstrates three stages for stabilization of the protein structure. The first two stages have a minor impact on lysozyme stability and ar
Publikováno v:
Biotechnology Letters. 36:869-875
Formulation scientists employed in the biopharmaceutical industry face the challenge of creating liquid aqueous formulations for proteins that never had evolutionary pressure to be exceptionally stable or soluble. Yet commercial products usually need
Autor:
Robert J. Falconer, Jordan W. Bye, Denis Ferachou, J. Axel Zeitler, Gianfelice Cinque, Stefano C. Meliga
Publikováno v:
The Journal of Physical Chemistry A. 118:83-88
Terahertz spectroscopy was used to study the absorption of bovine serum albumin (BSA) in water. The Diamond Light Source operating in a low alpha mode generated coherent synchrotron radiation that covered a useable spectral bandwidth of 0.3-3.3 THz (
Autor:
Robert J. Falconer, Jordan W. Bye
Publikováno v:
Protein Science. 22:1563-1570
Anion and cation effects on the structural stability of lysozyme were investigated using differential scanning calorimetry. At low concentrations (