Ultraviolet Raman spectroscopy is uniquely suitable for studying amyloid diseases
Amyloid fibrils associated with numerous degenerative diseases are non-crystalline and insoluble, and thus are not amenable to conventional X-ray crystallography and solution NMR, the classical tools of structural biology. We have recently demonstrated that deep UV resonance Raman (DUVRR) spectrosco...
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Veröffentlicht in: | Current science (Bangalore) 2009-07, Vol.97 (2), p.180-185 |
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creator | Lednev, Igor K. Shashilov, Victor Xu, Ming |
description | Amyloid fibrils associated with numerous degenerative diseases are non-crystalline and insoluble, and thus are not amenable to conventional X-ray crystallography and solution NMR, the classical tools of structural biology. We have recently demonstrated that deep UV resonance Raman (DUVRR) spectroscopy combined with hydrogen–deuterium exchange and advanced statistical analysis, 2D correlation in particular, allow for quantitative characterization of protein structural evolution at all stages of fibrillation in vitro. The application of DUVRR spectroscopy for studying the fibrillation of lysozyme is briefly overviewed here. |
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We have recently demonstrated that deep UV resonance Raman (DUVRR) spectroscopy combined with hydrogen–deuterium exchange and advanced statistical analysis, 2D correlation in particular, allow for quantitative characterization of protein structural evolution at all stages of fibrillation in vitro. The application of DUVRR spectroscopy for studying the fibrillation of lysozyme is briefly overviewed here.</description><identifier>ISSN: 0011-3891</identifier><language>eng</language><publisher>Current Science Association</publisher><subject>Aggregation ; Alzheimers disease ; Amides ; Amyloids ; Fibrillation ; Prion diseases ; Raman scattering ; Raman spectroscopy ; Solar fibrils ; SPECIAL SECTION: RAMAN SPECTROSCOPY ; Spectroscopy</subject><ispartof>Current science (Bangalore), 2009-07, Vol.97 (2), p.180-185</ispartof><rights>2009 Current Science Association</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/24111914$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/24111914$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,803,58015,58248</link.rule.ids></links><search><creatorcontrib>Lednev, Igor K.</creatorcontrib><creatorcontrib>Shashilov, Victor</creatorcontrib><creatorcontrib>Xu, Ming</creatorcontrib><title>Ultraviolet Raman spectroscopy is uniquely suitable for studying amyloid diseases</title><title>Current science (Bangalore)</title><description>Amyloid fibrils associated with numerous degenerative diseases are non-crystalline and insoluble, and thus are not amenable to conventional X-ray crystallography and solution NMR, the classical tools of structural biology. We have recently demonstrated that deep UV resonance Raman (DUVRR) spectroscopy combined with hydrogen–deuterium exchange and advanced statistical analysis, 2D correlation in particular, allow for quantitative characterization of protein structural evolution at all stages of fibrillation in vitro. The application of DUVRR spectroscopy for studying the fibrillation of lysozyme is briefly overviewed here.</description><subject>Aggregation</subject><subject>Alzheimers disease</subject><subject>Amides</subject><subject>Amyloids</subject><subject>Fibrillation</subject><subject>Prion diseases</subject><subject>Raman scattering</subject><subject>Raman spectroscopy</subject><subject>Solar fibrils</subject><subject>SPECIAL SECTION: RAMAN SPECTROSCOPY</subject><subject>Spectroscopy</subject><issn>0011-3891</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNotj8tqwzAQRb1ooWnaTyho1Z1BI9mKtSyhLwiElmZtJnoUBdlyNXLBf99Aujqbw-Heq2rFOUAtOw031S3RiXMhBder6uMQS8bfkKIr7BMHHBlNzpScyKRpYYHYPIaf2cWF0RwKHqNjPmVGZbZLGL8ZDktMwTIbyCE5uquuPUZy9_9cV4eX56_tW73bv75vn3b1SfCu1NpY3DQW_FFy1YL2zmyMtlrpVnoJnneA3Fgljp1Srm3EBhvVtAjKS4OOy3X1eOlOOZ33UemHQMbFiKNLM_UCxPmzEmfx4SKeqKTcTzkMmJdeNACgoZF_8_NW6w</recordid><startdate>20090725</startdate><enddate>20090725</enddate><creator>Lednev, Igor K.</creator><creator>Shashilov, Victor</creator><creator>Xu, Ming</creator><general>Current Science Association</general><scope>7TK</scope></search><sort><creationdate>20090725</creationdate><title>Ultraviolet Raman spectroscopy is uniquely suitable for studying amyloid diseases</title><author>Lednev, Igor K. ; Shashilov, Victor ; Xu, Ming</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j208t-9cda74d1fb306519fec7c9d96953f31f081a0cd62b866e5427a4645a16f3cae03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Aggregation</topic><topic>Alzheimers disease</topic><topic>Amides</topic><topic>Amyloids</topic><topic>Fibrillation</topic><topic>Prion diseases</topic><topic>Raman scattering</topic><topic>Raman spectroscopy</topic><topic>Solar fibrils</topic><topic>SPECIAL SECTION: RAMAN SPECTROSCOPY</topic><topic>Spectroscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lednev, Igor K.</creatorcontrib><creatorcontrib>Shashilov, Victor</creatorcontrib><creatorcontrib>Xu, Ming</creatorcontrib><collection>Neurosciences Abstracts</collection><jtitle>Current science (Bangalore)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lednev, Igor K.</au><au>Shashilov, Victor</au><au>Xu, Ming</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ultraviolet Raman spectroscopy is uniquely suitable for studying amyloid diseases</atitle><jtitle>Current science (Bangalore)</jtitle><date>2009-07-25</date><risdate>2009</risdate><volume>97</volume><issue>2</issue><spage>180</spage><epage>185</epage><pages>180-185</pages><issn>0011-3891</issn><abstract>Amyloid fibrils associated with numerous degenerative diseases are non-crystalline and insoluble, and thus are not amenable to conventional X-ray crystallography and solution NMR, the classical tools of structural biology. We have recently demonstrated that deep UV resonance Raman (DUVRR) spectroscopy combined with hydrogen–deuterium exchange and advanced statistical analysis, 2D correlation in particular, allow for quantitative characterization of protein structural evolution at all stages of fibrillation in vitro. The application of DUVRR spectroscopy for studying the fibrillation of lysozyme is briefly overviewed here.</abstract><pub>Current Science Association</pub><tpages>6</tpages></addata></record> |
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source | Free E-Journal (出版社公開部分のみ); JSTOR |
subjects | Aggregation Alzheimers disease Amides Amyloids Fibrillation Prion diseases Raman scattering Raman spectroscopy Solar fibrils SPECIAL SECTION: RAMAN SPECTROSCOPY Spectroscopy |
title | Ultraviolet Raman spectroscopy is uniquely suitable for studying amyloid diseases |
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