Search Results - "Austerberry, James I."

Arginine to Lysine Mutations Increase the Aggregation Stability of a Single-Chain Variable Fragment through Unfolded-State Interactions by Austerberry, James I, Thistlethwaite, Angela, Fisher, Karl, Golovanov, Alexander P, Pluen, Alain, Esfandiary, Reza, van der Walle, Christopher F, Warwicker, Jim, Derrick, Jeremy P, Curtis, Robin

“…Increased protein solubility is known to correlate with an increase in the proportion of lysine over arginine residues. Previous work has shown that the…”
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The effect of charge mutations on the stability and aggregation of a human single chain Fv fragment by Austerberry, James I., Dajani, Rana, Panova, Stanislava, Roberts, Dorota, Golovanov, Alexander P., Pluen, Alain, van der Walle, Christopher F., Uddin, Shahid, Warwicker, Jim, Derrick, Jeremy P., Curtis, Robin

“…[Display omitted] The aggregation propensities for a series of single-chain variable fragment (scFv) mutant proteins containing supercharged sequences, salt…”
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Identification of B cell epitopes enhanced by protein unfolding and aggregation by Eyes, Timothy J., Austerberry, James I., Dearman, Rebecca J., Johannissen, Linus O., Kimber, Ian, Smith, Noel, Thistlethwaite, Angela, Derrick, Jeremy P.

“…•Aggregation of an exemplar therapeutic antibody fragment (scFv) enhances immunogenicity in vivo.•Epitope mapping reveals immunogenicity is directed to a…”
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Proofreading of substrate structure by the Twin-Arginine Translocase is highly dependent on substrate conformational flexibility but surprisingly tolerant of surface charge and hydrophobicity changes by Jones, Alexander S., Austerberry, James I., Dajani, Rana, Warwicker, Jim, Curtis, Robin, Derrick, Jeremy P., Robinson, Colin

“…The Tat system transports folded proteins across the bacterial plasma membrane, and in Escherichia coli preferentially transports correctly-folded proteins…”
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The aggregation of cytochrome C may be linked to its flexibility during refolding by Austerberry, James I., Belton, Daniel J.

“…Large-scale expression of biopharmaceutical proteins in cellular hosts results in production of large insoluble mass aggregates. In order to generate…”
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The aggregation of cytochrome C may be linked to its flexibility during refolding by Austerberry, James I, Belton, Daniel J

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