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Article: Study of oat globulin conformation by Fourier transform infrared spectroscopy

TitleStudy of oat globulin conformation by Fourier transform infrared spectroscopy
Authors
KeywordsDenaturation
FTIR spectroscopy
Oat globulin
Protein conformation
Issue Date2001
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 2001, v. 49 n. 7, p. 3328-3334 How to Cite?
AbstractThe conformation of oat globulin dispersions (10% in D 2O) under the influence of pH, chaotropic salts, protein structure perturbants, and heating conditions was studied by Fourier transform infrared (FTIR) spectroscopy. The FTIR spectrum of oat globulin showed major bands from 1670 to 1634 cm -1, corresponding to the four major types of secondary structures, that is, β-turns, β-sheets, α-helices, and random coils. At extreme acidic and alkaline pH conditions, there were changes in intensity in the bands attributed to β-sheet structures (1626, 1634, and 1682 cm -1), and shifts of the bands to higher or lower wavenumbers, indicating changes in conformation. In the presence of some chaotropic salts, the 1626 and 1634 cm -1 bands were shifted upward, with a marked decrease in the intensity of the 1634 cm -1 peak. The addition of several protein structure perturbants led to a slight shift in the α-helix/random coil bands and a marked reduction in the β-sheet peaks, suggesting protein unfolding. Heating under aggregating conditions led to slight shifts in all of the major bands and progressive changes in the intensity of the α-helix, β-sheet, and β-turn peaks, suggesting protein denaturation. This was accompanied by marked increases in intensity of the two intermolecular β-sheet bands (1682 and 1624-1626 cm -1) associated with the formation of aggregated strands. The IR spectra of soluble and insoluble aggregates showed a redistribution of native and extensively denatured proteins in the two fractions.
Persistent Identifierhttp://hdl.handle.net/10722/68415
ISSN
2015 Impact Factor: 2.857
2015 SCImago Journal Rankings: 1.246
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMa, CYen_HK
dc.contributor.authorRout, MKen_HK
dc.contributor.authorMock, WYen_HK
dc.date.accessioned2010-09-06T06:04:25Z-
dc.date.available2010-09-06T06:04:25Z-
dc.date.issued2001en_HK
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 2001, v. 49 n. 7, p. 3328-3334en_HK
dc.identifier.issn0021-8561en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68415-
dc.description.abstractThe conformation of oat globulin dispersions (10% in D 2O) under the influence of pH, chaotropic salts, protein structure perturbants, and heating conditions was studied by Fourier transform infrared (FTIR) spectroscopy. The FTIR spectrum of oat globulin showed major bands from 1670 to 1634 cm -1, corresponding to the four major types of secondary structures, that is, β-turns, β-sheets, α-helices, and random coils. At extreme acidic and alkaline pH conditions, there were changes in intensity in the bands attributed to β-sheet structures (1626, 1634, and 1682 cm -1), and shifts of the bands to higher or lower wavenumbers, indicating changes in conformation. In the presence of some chaotropic salts, the 1626 and 1634 cm -1 bands were shifted upward, with a marked decrease in the intensity of the 1634 cm -1 peak. The addition of several protein structure perturbants led to a slight shift in the α-helix/random coil bands and a marked reduction in the β-sheet peaks, suggesting protein unfolding. Heating under aggregating conditions led to slight shifts in all of the major bands and progressive changes in the intensity of the α-helix, β-sheet, and β-turn peaks, suggesting protein denaturation. This was accompanied by marked increases in intensity of the two intermolecular β-sheet bands (1682 and 1624-1626 cm -1) associated with the formation of aggregated strands. The IR spectra of soluble and insoluble aggregates showed a redistribution of native and extensively denatured proteins in the two fractions.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcauen_HK
dc.relation.ispartofJournal of Agricultural and Food Chemistryen_HK
dc.subjectDenaturationen_HK
dc.subjectFTIR spectroscopyen_HK
dc.subjectOat globulinen_HK
dc.subjectProtein conformationen_HK
dc.titleStudy of oat globulin conformation by Fourier transform infrared spectroscopyen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-8561&volume=49&spage=3328&epage=3334&date=2001&atitle=Study+of+oat+globulin+conformation+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.doi10.1021/jf010053fen_HK
dc.identifier.pmid11453771-
dc.identifier.scopuseid_2-s2.0-0034852941en_HK
dc.identifier.hkuros61571en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034852941&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume49en_HK
dc.identifier.issue7en_HK
dc.identifier.spage3328en_HK
dc.identifier.epage3334en_HK
dc.identifier.isiWOS:000170043400030-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.scopusauthoridRout, MK=16036793300en_HK
dc.identifier.scopusauthoridMock, WY=7005314640en_HK

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