17969139

Source:http://linkedlifedata.com/resource/pubmed/id/17969139

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0014834, umls-concept:C0040709, umls-concept:C0205360, umls-concept:C0220825, umls-concept:C0439855, umls-concept:C0678594, umls-concept:C1704259, umls-concept:C1705987
pubmed:issue	6
pubmed:dateCreated	2008-3-4
pubmed:abstractText	We have previously developed a rapid microplate-based approach for measuring the denaturation curves by intrinsic tryptophan fluorescence for simple monomeric and two-state unfolding proteins. Here we demonstrate that it can accurately resolve the multiple conformational transitions that occur during the denaturation of a complex multimeric and cofactor associated protein. We have also analyzed the effect of two active-site mutations, D381A and Y440A upon the denaturation pathway of transketolase using intrinsic fluorescence measurements, and we compare the results from classical and microplate-based instrumentation. This work shows that the rapid assay is able to identify changes in the denaturation pathway, due to mutations or removal of cofactors, which affect the stability of the native and intermediate states. This would be of significant benefit for the directed evolution of protein stability, optimizing enzyme stability under biocatalytic process conditions, and also for engineering specific transitions in protein unfolding pathways.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7502021
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Transketolase
pubmed:status	MEDLINE
pubmed:month	Apr
pubmed:issn	1097-0290
pubmed:author	pubmed-author:AucampJean PJP, pubmed-author:DalbyPaul APA, pubmed-author:HibbertEdward GEG, pubmed-author:Martinez-TorresRuben JRJ
pubmed:copyrightInfo	Copyright 2007 Wiley Periodicals, Inc.
pubmed:issnType	Electronic
pubmed:day	15
pubmed:volume	99
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1303-10
pubmed:meshHeading	pubmed-meshheading:17969139-Enzyme Stability, pubmed-meshheading:17969139-Escherichia coli, pubmed-meshheading:17969139-Protein Array Analysis, pubmed-meshheading:17969139-Protein Denaturation, pubmed-meshheading:17969139-Signal Transduction, pubmed-meshheading:17969139-Transketolase
pubmed:year	2008
pubmed:articleTitle	A microplate-based evaluation of complex denaturation pathways: structural stability of Escherichia coli transketolase.
pubmed:affiliation	The Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, University College London, Torrington Place, London WC1E 7JE, UK.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't