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dc.contributor.authorDuke, EM
dc.contributor.authorHadfield, A
dc.contributor.authorMartin, JL
dc.contributor.authorClifton, IJ
dc.contributor.authorHajdu, J
dc.contributor.authorJohnson, LN
dc.contributor.authorReid, GP
dc.contributor.authorTrentham, DR
dc.contributor.authorBruce, I
dc.contributor.authorFleet, GW
dc.contributor.editorChadwick D.J and Widdows K.
dc.date.accessioned2018-07-17T04:39:10Z
dc.date.available2018-07-17T04:39:10Z
dc.date.issued1991
dc.identifier.isbn9780471929697
dc.identifier.doi10.1002/9780470514146.ch6
dc.identifier.urihttp://hdl.handle.net/10072/378705
dc.description.abstractLaue diffraction with high intensity, broad‐spectrum synchrotron radiation sources allows three‐dimensional data sets on protein crystals to be recorded in seconds or milliseconds and opens the way for time‐resolved studies on dynamic events in crystals. This chapter briefly reviews the field and describes progress towards time‐resolved studies with glycogen phosphorylase. Methods for the synchronization of the start of reaction with the start of data collection have been developed for the phosphorolytic reaction of glycogen phosphorylase. The compound 3,5‐dinitrophenylphosphate is photolabile, yielding Pi and the by‐product, 3,5‐dinitrophenol, which is non‐reactive with the enzyme. Spectroscopic studies show that the compound has good quantum yield and that photolysis is rapid (> 1000 s−1). Release of the dinitrophenylate anion, following a pulse of light from a xenon flash lamp, has been monitored with a diode array spectrophotometer specially adapted for measurements on crystals. In a laboratory X‐ray experiment with crystals of glycogen phosphorylase b, release of Pi and formation of the enzyme–product complex have been demonstrated. The way is now open for Laue diffraction studies on the catalytic reaction in the crystal.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherJohn Wiley and Sons Ltd
dc.publisher.placeUnited Kingdom
dc.relation.ispartofbooktitleProtein Conformation. Ciba Foundation Symposium 161
dc.relation.ispartofchapter6
dc.relation.ispartofpagefrom75
dc.relation.ispartofpageto90
dc.relation.ispartofedition1st
dc.relation.ispartofvolume161
dc.subject.fieldofresearchBiochemistry and Cell Biology not elsewhere classified
dc.subject.fieldofresearchcode060199
dc.titleTowards Time-Resolved Diffraction Studies with Glycogen Phosphorylase
dc.typeBook chapter
dc.type.descriptionB1 - Chapters
dc.type.codeB - Book Chapters
gro.hasfulltextNo Full Text
gro.griffith.authorMartin, Jennifer


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