Anisotropy resolved multidimensional emission spectroscopy (ARMES): A new tool for protein analysis
dc.contributor.author | Groza, Radu Constantin | |
dc.contributor.author | Ryder, Alan G. | |
dc.contributor.author | Li, Boyan | |
dc.date.accessioned | 2016-01-29T21:19:37Z | |
dc.date.issued | 2015-07-30 | |
dc.identifier.citation | Groza, RC; Li, BY; Ryder, AG; (2015) 'Anisotropy resolved multidimensional emission spectroscopy (ARMES): A new tool for protein analysis'. Analytica chimica acta, 886 :133-142. | en_IE |
dc.identifier.issn | 1873-4324 | |
dc.identifier.uri | http://hdl.handle.net/10379/5507 | |
dc.description.abstract | Structural analysis of proteins using the emission of intrinsic fluorophores is complicated by spectral overlap. Anisotropy resolved multidimensional emission spectroscopy (ARMES) overcame the overlap problem by the use of anisotropy, with chemometric analysis, to better resolve emission from different fluorophores. Total synchronous fluorescence scan (TSFS) provided information about all the fluorophores that contributed to emission while anisotropy provided information about the environment of each fluorophore. Here the utility of ARMES was demonstrated via study of the chemical and thermal denaturation of human serum albumin (HSA).Multivariate curve resolution (MCR) analysis of the constituent polarized emission ARMES data resolved contributions from four emitters: fluorescence from tryptophan (Trp), solvent exposed tyrosine (Tyr), Tyr in a hydrophobic environment, and room temperature phosphorescence (RTP) from Trp. The MCR scores, anisotropy, and literature validated these assignments and showed all the expected transitions during HSA unfolding. This new methodology for comprehensive intrinsic fluorescence analysis of proteins is applicable to any protein containing multiple fluorophores. (C) 2015 Elsevier B.V. All rights reserved. | en_IE |
dc.description.sponsorship | RCG was supported by an ‘EMBARK Initiative’ Postgraduate Scholarship from the Irish Research Council | en_IE |
dc.format | application/pdf | en_IE |
dc.language.iso | en | en_IE |
dc.publisher | Elsevier | en_IE |
dc.relation.ispartof | Analytica chimica acta | en |
dc.subject | Fluorescence | en_IE |
dc.subject | Anisotropy | en_IE |
dc.subject | Multidimensional | en_IE |
dc.subject | Protein | en_IE |
dc.subject | Unfolding | en_IE |
dc.subject | Chemometrics | en_IE |
dc.subject | Human-serum-albumin | en_IE |
dc.subject | Cell culture media | en_IE |
dc.subject | Multivariate curve resolution | en_IE |
dc.subject | Principal component analysis | en_IE |
dc.subject | Fluorescence spectroscopy | en_IE |
dc.subject | Noise perturbation | en_IE |
dc.subject | Crystal-structure | en_IE |
dc.subject | Practical aspects | en_IE |
dc.subject | EEM spectroscopy | en_IE |
dc.subject | Low temperatures | en_IE |
dc.subject | Chemistry | en_IE |
dc.title | Anisotropy resolved multidimensional emission spectroscopy (ARMES): A new tool for protein analysis | en_IE |
dc.type | Article | en_IE |
dc.date.updated | 2015-12-22T16:39:55Z | |
dc.identifier.doi | 10.1016/j.aca.2015.06.011 | |
dc.local.publishedsource | http://dx.doi.org/10.1016/j.aca.2015.06.011 | en_IE |
dc.description.peer-reviewed | peer-reviewed | |
dc.contributor.funder | |~|6201984|~| | |
dc.description.embargo | 2017-07-30 | |
dc.internal.rssid | 9878581 | |
dc.local.contact | Alan Ryder, School Of Chemistry, Room 213, Arts/Science Building, Nui Galway. 2943 Email: alan.ryder@nuigalway.ie | |
dc.local.copyrightchecked | No | |
dc.local.version | ACCEPTED | |
nui.item.downloads | 285 |
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