Search Results - "Chung, Evonne W"

Probing the Nature of Noncovalent Interactions by Mass Spectrometry. A Study of Protein−CoA Ligand Binding and Assembly by Robinson, Carol V, Chung, Evonne W, Kragelund, Birthe B, Knudsen, Jens, Aplin, Robin T, Poulsen, Flemming M, Dobson, Christopher M

“…A series of noncovalent complexes formed between the 86 residue acyl CoA binding protein (ACBP) and a series of acyl CoA derivatives has been studied by…”
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High-throughput screening of corticosteroids and basic drugs in horse urine by liquid chromatography-tandem mass spectrometry by Leung, Gary N.W., Chung, Evonne W., Ho, Emmie N.M., Kwok, W.H., Leung, David K.K., Tang, Francis P.W., Wan, Terence S.M., Yu, Nola H.

“…This paper describes two high-throughput liquid chromatography-tandem mass spectrometry (LC-MS-MS) methods for the screening of two important classes of drugs…”
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The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase by van den Berg, Bert, Chung, Evonne W., Robinson, Carol V., Mateo, Pedro L., Dobson, Christopher M.

“…The oxidative refolding of hen lysozyme has been studied by a variety of time‐resolved biophysical methods in conjunction with analysis of folding…”
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The origin of the α-domain intermediate in the folding of hen lysozyme by Matagne, André, Chung, Evonne W, Ball, Linda J, Radford, Sheena E, Robinson, Carol V, Dobson, Christopher M

“…Stopped-flow fluorescence and circular dichroism spectroscopy have been used in conjunction with quenched-flow hydrogen exchange labelling, monitored by…”
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Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain by Krebs, Mark R.H, Wilkins, Deborah K, Chung, Evonne W, Pitkeathly, Maureen C, Chamberlain, Aaron K, Zurdo, Jesus, Robinson, Carol V, Dobson, Christopher M

“…Wild-type hen lysozyme has been converted from its soluble native state into highly organized amyloid fibrils. In order to achieve this conversion, conditions…”
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Characterisation of the dominant oxidative folding intermediate of hen lysozyme by Van den Berg, B, Chung, E.W, Robinson, C.V, Dobson, C.M

“…Reduced denatured lysozyme has been oxidised and refolded at pH values close to neutral in an efficient way by dilution from buffers containing 8.0 M urea, and…”
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Thermal unfolding of an intermediate is associated with non-arrhenius kinetics in the folding of hen lysozyme by Matagne, André, Jamin, Marc, Chung, Evonne W., Robinson, Carol V., Radford, Sheena E., Dobson, Christopher M.

“…A variety of techniques, including quenched-flow hydrogen exchange labelling monitored by electrospray ionization mass spectrometry, and stopped-flow…”
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Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB by GROß, MICHAEL, WILKINS, DEBORAH K., PITKEATHLY, MAUREEN C., CHUNG, EVONNE W., HIGHAM, CLAIRE, CLARK, ANNE, DOBSON, CHRISTOPHER M.

“…Three peptides covering the sequence regions corresponding to the first two (CspB-1), the first three (CspB-2), and the last two (CspB-3) β-strands of CspB,…”
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Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR by Chung, Evonne W., Nettleton, Ewan J., Morgan, Charles J., Groß, Michael, Miranker, Andrew, Radford, Sheena E., Dobson, Christopher M., Robinson, Carol V.

“…The extent of deuterium labeling of hen lysozyme, its three‐disulfide derivative, and the homologous α‐lactalbumins, has been measured by both mass…”
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Probing the nature of interactions in SH2 binding interfaces—Evidence from electrospray ionization mass spectrometry by CHUNG, EVONNE W., HENRIQUES, DENISE A., RENZONI, DEBORA, MORTON, CRAIG J., MULHERN, TERRENCE D., PITKEATHLY, MAUREEN C., LADBURY, JOHN E., ROBINSON, CAROL V.

“…We have adopted nanoflow electrospray ionization mass spectrometry (ESI-MS) and isothermal titration calorimetry (ITC) to probe the mechanism of peptide…”
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Characterisation of the dominant oxidative folding intermediate of hen lysozyme 1 1Edited by P. E. Wright by van den Berg, Bert, Chung, Evonne W., Robinson, Carol V., Dobson, Christopher M.

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