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Article: Raman spectroscopic study of oat globulin conformation

TitleRaman spectroscopic study of oat globulin conformation
Authors
Ma, CYRout, MKChan, WMPhillips, DL
KeywordsOat globulin
Protein conformation
Raman spectroscopy
Issue Date2000
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 2000, v. 48 n. 5, p. 1542-1547 How to Cite?
DOI: http://dx.doi.org/10.1021/jf991222n
AbstractAnalysis of Raman spectra of oat globulin showed that extreme pH values caused an increase in the amide and C-H stretching band intensity, indicating changes in the secondary structures of the protein due to denaturation. Similar changes were observed when oat globulin was treated with chaotropic salts and several protein perturbants. Sodium dodecyl sulfate, β- mercaptoethanol, and ethylene glycol also caused a shift in the amide III' band, suggesting a transition from β-sheet to a random coil conformation. Heating at temperatures near the denaturation temperature of oat globulin led to increases in the amide and C-H band intensity, indicating unfolding of the protein. The data indicate that FT-Raman spectroscopy is suitable for studying the secondary structure of plant proteins such as oat globulin.
Persistent Identifierhttp://hdl.handle.net/10722/68553
ISSN
0021-8561
2023 Impact Factor: 5.7
2023 SCImago Journal Rankings: 1.114
ISI Accession Number ID
WOS:000087116000020
References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorMa, CYen_HK
dc.contributor.authorRout, MKen_HK
dc.contributor.authorChan, WMen_HK
dc.contributor.authorPhillips, DLen_HK
dc.date.accessioned2010-09-06T06:05:38Z-
dc.date.available2010-09-06T06:05:38Z-
dc.date.issued2000en_HK
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 2000, v. 48 n. 5, p. 1542-1547en_HK
dc.identifier.issn0021-8561en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68553-
dc.description.abstractAnalysis of Raman spectra of oat globulin showed that extreme pH values caused an increase in the amide and C-H stretching band intensity, indicating changes in the secondary structures of the protein due to denaturation. Similar changes were observed when oat globulin was treated with chaotropic salts and several protein perturbants. Sodium dodecyl sulfate, β- mercaptoethanol, and ethylene glycol also caused a shift in the amide III' band, suggesting a transition from β-sheet to a random coil conformation. Heating at temperatures near the denaturation temperature of oat globulin led to increases in the amide and C-H band intensity, indicating unfolding of the protein. The data indicate that FT-Raman spectroscopy is suitable for studying the secondary structure of plant proteins such as oat globulin.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.subjectOat globulinen_HK
dc.subjectProtein conformationen_HK
dc.subjectRaman spectroscopyen_HK
dc.titleRaman spectroscopic study of oat globulin conformationen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-8561&volume=48&spage=1542&epage=1547&date=2000&atitle=Raman+spectroscopic+study+of+oat+globulin+conformationen_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.emailPhillips, DL: phillips@hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.identifier.authorityPhillips, DL=rp00770en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/jf991222nen_HK
dc.identifier.pmid10820056-
dc.identifier.scopuseid_2-s2.0-0034115577en_HK
dc.identifier.hkuros51204en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034115577&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume48en_HK
dc.identifier.issue5en_HK
dc.identifier.spage1542en_HK
dc.identifier.epage1547en_HK
dc.identifier.isiWOS:000087116000020-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.scopusauthoridRout, MK=16036793300en_HK
dc.identifier.scopusauthoridChan, WM=55471369000en_HK
dc.identifier.scopusauthoridPhillips, DL=7404519365en_HK
dc.identifier.issnl0021-8561-

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