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Article: Conformational study of globulin from rice (Oryza sativa) seeds by Fourier-transform infrared spectroscopy

TitleConformational study of globulin from rice (Oryza sativa) seeds by Fourier-transform infrared spectroscopy
Authors
KeywordsAggregation
Denaturation
FTIR spectroscopy
Protein conformation
Rice globulin
Issue Date2005
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ijbiomac
Citation
International Journal Of Biological Macromolecules, 2005, v. 37 n. 1-2, p. 12-20 How to Cite?
AbstractThe conformation of rice globulin (10%, w/v, in deuterated phosphate buffer, pD 7.4) under the influence of pH, chaotropic salts, several protein structure perturbants and heat treatments was studied by Fourier-transform infrared (FTIR) spectroscopy. Rice globulin exhibited seven major bands in the region of 1700-1600 cm -1 and the spectrum suggests high α-helical content with large quantities of β-sheet and β-turn structures. Highly acidic and alkaline pH conditions induced changes in band intensity attributed to intermolecular β-sheet structure (1681 and 1619 cm -1). Addition of chaotropic salts led to progressive changes in band intensity, following the lyotropic series of anions, whereas several protein structure perturbants caused shifts in band positions. Heating at increasing temperature led to progressive decreases in α-helical content and increases in random coil structures, suggesting protein denaturation. This was accompanied by intensity increases in the intermolecular β-sheet transitions. © 2005 Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68639
ISSN
2015 Impact Factor: 3.138
2015 SCImago Journal Rankings: 0.815
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorEllepola, SWen_HK
dc.contributor.authorSiu, MCen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:06:22Z-
dc.date.available2010-09-06T06:06:22Z-
dc.date.issued2005en_HK
dc.identifier.citationInternational Journal Of Biological Macromolecules, 2005, v. 37 n. 1-2, p. 12-20en_HK
dc.identifier.issn0141-8130en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68639-
dc.description.abstractThe conformation of rice globulin (10%, w/v, in deuterated phosphate buffer, pD 7.4) under the influence of pH, chaotropic salts, several protein structure perturbants and heat treatments was studied by Fourier-transform infrared (FTIR) spectroscopy. Rice globulin exhibited seven major bands in the region of 1700-1600 cm -1 and the spectrum suggests high α-helical content with large quantities of β-sheet and β-turn structures. Highly acidic and alkaline pH conditions induced changes in band intensity attributed to intermolecular β-sheet structure (1681 and 1619 cm -1). Addition of chaotropic salts led to progressive changes in band intensity, following the lyotropic series of anions, whereas several protein structure perturbants caused shifts in band positions. Heating at increasing temperature led to progressive decreases in α-helical content and increases in random coil structures, suggesting protein denaturation. This was accompanied by intensity increases in the intermolecular β-sheet transitions. © 2005 Elsevier B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ijbiomacen_HK
dc.relation.ispartofInternational Journal of Biological Macromoleculesen_HK
dc.rightsInternational Journal of Biological Macromolecules. Copyright © Elsevier BV.en_HK
dc.subjectAggregationen_HK
dc.subjectDenaturationen_HK
dc.subjectFTIR spectroscopyen_HK
dc.subjectProtein conformationen_HK
dc.subjectRice globulinen_HK
dc.titleConformational study of globulin from rice (Oryza sativa) seeds by Fourier-transform infrared spectroscopyen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0141-8130&volume=37&spage=12&epage=20&date=2005&atitle=Conformational+study+of+globulin+from+rice+(Oryza+sativa)+seeds+by+Fourier-transform+infrared+spectroscopyen_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.ijbiomac.2005.07.008en_HK
dc.identifier.pmid16140371en_HK
dc.identifier.scopuseid_2-s2.0-27544467437en_HK
dc.identifier.hkuros115300en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-27544467437&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume37en_HK
dc.identifier.issue1-2en_HK
dc.identifier.spage12en_HK
dc.identifier.epage20en_HK
dc.identifier.isiWOS:000233283800002-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridEllepola, SW=9843111000en_HK
dc.identifier.scopusauthoridSiu, MC=8959662100en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK

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