Combining UV Absorbance and Diagnostic CID Fragment Ions to Identify and Distinguish Isobaric Chromophores on Phycobiliproteins

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dc.contributor.authorLoubna Hammad
dc.contributor.authorAnimesh Shukla
dc.contributor.authorAvijit Biswas
dc.contributor.authorYuening Zhang
dc.contributor.authorDavid Kehoe
dc.contributor.authorWendy Schluchter
dc.contributor.authorJonathan A. Karty
dc.date.accessioned2017-05-03T09:36:43Z
dc.date.available2017-05-03T09:36:43Z
dc.date.issued2011-06-01
dc.description.abstract<p>Certain cyanobacteria change the tetrapyrrole pigments attached to phycoerythrin inresponse to the color of light available. These tetrapyrrole pigments consist ofphycoerythrobilin (PEB) and phycourobilin (PUB) which are structural isomers PEB andPUB differ in the position of one double bond and are therefore isobaric but have differentUV-absorbance spectra. Each phycobiliprotein may have several bilin pigments attached tovarious cysteine residues. Researchers purify microgram amounts of protein to performHPLC-UV-VIS experiments to identify the pigments utilized by the organism. The pigmentsattached to phycoerythrins produced in green vs blue light in Synechococcus RS 9916 havenot been determined. This work utilizes the CID fragmentation patterns of differentbilipeptides in conjunction with UV-absorbance to facilitate pigment attachment siteidentifications.</p>en
dc.description.abstract<p>Certain cyanobacteria change the tetrapyrrole pigments attached to phycoerythrin inresponse to the color of light available. These tetrapyrrole pigments consist ofphycoerythrobilin (PEB) and phycourobilin (PUB) which are structural isomers PEB andPUB differ in the position of one double bond and are therefore isobaric but have differentUV-absorbance spectra. Each phycobiliprotein may have several bilin pigments attached tovarious cysteine residues. Researchers purify microgram amounts of protein to performHPLC-UV-VIS experiments to identify the pigments utilized by the organism. The pigmentsattached to phycoerythrins produced in green vs blue light in Synechococcus RS 9916 havenot been determined. This work utilizes the CID fragmentation patterns of differentbilipeptides in conjunction with UV-absorbance to facilitate pigment attachment siteidentifications.</p>ar
dc.identifier.urihttps://hdl.handle.net/20.500.11888/9491
dc.titleCombining UV Absorbance and Diagnostic CID Fragment Ions to Identify and Distinguish Isobaric Chromophores on Phycobiliproteinsen
dc.titleCombining UV Absorbance and Diagnostic CID Fragment Ions to Identify and Distinguish Isobaric Chromophores on Phycobiliproteinsar
dc.typeOther
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The Fifth Palestinian International Chemistry Conference