File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Fourier-transform infrared spectroscopic study of globulin from Phaseolus angularis (red bean)

TitleFourier-transform infrared spectroscopic study of globulin from Phaseolus angularis (red bean)
Authors
KeywordsAggregation
Denaturation
FTIR spectroscopy
Protein conformation
Red bean globulin
Issue Date2001
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ijbiomac
Citation
International Journal Of Biological Macromolecules, 2001, v. 29 n. 4-5, p. 287-294 How to Cite?
AbstractThe conformation of red bean globulin dispersions (≈10% in D2O or deuterated phosphate buffer pD 7.4) 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 red bean globulin showed major bands from 1682 to 1637 cm-1 in the amide I′ region, corresponding to the four types of secondary structures, i.e. β-turns, β-sheets, α-helix and random coils. At extreme pH conditions, there were changes in intensity in bands attributed to β-sheet (1637 and 1618 cm-1) and random coil (1644 cm-1) structures, and shifts of these bands to lower or higher wavenumbers, indicating changes in protein conformation. Chaotropic salts caused progressive increases in random coil structures and concomitant decreases in β-sheet bands, following the lyotrophic series of anions. In the presence of sodium dodecyl sulfate and ethylene glycol, pronounced increases in the random coil band were observed, accompanied by slight shifts of the β-sheet band. Addition of dithiothreitol and N-ethylmaleimide did not cause marked changes in the FTIR spectra. Heating at increasing temperature led to progressive decreases in the intensity of the α-helix and β-sheet bands and increases in random coil band intensity, leveling off at around 60°C. The data suggest that re-organization of protein structure occurred at temperatures well below the denaturation temperature of red bean globulin (86°C) as determined by differential scanning calorimetry. This was accompanied by pronounced increases in the intensity of the two intermolecular β-sheet bands (1682 and 1619-1620 cm-1) associated with the formation of aggregated strands at higher temperatures (80-90°C). Increases in intensity of the aggregation bands were also observed in the heat-induced buffer-soluble and insoluble aggregates. Copyright © 2001 Elsevier Science B.V.
Persistent Identifierhttp://hdl.handle.net/10722/68453
ISSN
2015 Impact Factor: 3.138
2015 SCImago Journal Rankings: 0.815
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMeng, GTen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:04:45Z-
dc.date.available2010-09-06T06:04:45Z-
dc.date.issued2001en_HK
dc.identifier.citationInternational Journal Of Biological Macromolecules, 2001, v. 29 n. 4-5, p. 287-294en_HK
dc.identifier.issn0141-8130en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68453-
dc.description.abstractThe conformation of red bean globulin dispersions (≈10% in D2O or deuterated phosphate buffer pD 7.4) 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 red bean globulin showed major bands from 1682 to 1637 cm-1 in the amide I′ region, corresponding to the four types of secondary structures, i.e. β-turns, β-sheets, α-helix and random coils. At extreme pH conditions, there were changes in intensity in bands attributed to β-sheet (1637 and 1618 cm-1) and random coil (1644 cm-1) structures, and shifts of these bands to lower or higher wavenumbers, indicating changes in protein conformation. Chaotropic salts caused progressive increases in random coil structures and concomitant decreases in β-sheet bands, following the lyotrophic series of anions. In the presence of sodium dodecyl sulfate and ethylene glycol, pronounced increases in the random coil band were observed, accompanied by slight shifts of the β-sheet band. Addition of dithiothreitol and N-ethylmaleimide did not cause marked changes in the FTIR spectra. Heating at increasing temperature led to progressive decreases in the intensity of the α-helix and β-sheet bands and increases in random coil band intensity, leveling off at around 60°C. The data suggest that re-organization of protein structure occurred at temperatures well below the denaturation temperature of red bean globulin (86°C) as determined by differential scanning calorimetry. This was accompanied by pronounced increases in the intensity of the two intermolecular β-sheet bands (1682 and 1619-1620 cm-1) associated with the formation of aggregated strands at higher temperatures (80-90°C). Increases in intensity of the aggregation bands were also observed in the heat-induced buffer-soluble and insoluble aggregates. Copyright © 2001 Elsevier Science B.V.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.subjectRed bean globulinen_HK
dc.titleFourier-transform infrared spectroscopic study of globulin from Phaseolus angularis (red bean)en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0141-8130&volume=29&spage=287&epage=294&date=2001&atitle=Fourier-transform+infrared+spectroscopic+study+of+globulin+from+Phaseolus+angularis+(red+bean)en_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/S0141-8130(01)00178-7en_HK
dc.identifier.pmid11718826-
dc.identifier.scopuseid_2-s2.0-0035842073en_HK
dc.identifier.hkuros67997en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035842073&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume29en_HK
dc.identifier.issue4-5en_HK
dc.identifier.spage287en_HK
dc.identifier.epage294en_HK
dc.identifier.isiWOS:000172670700010-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridMeng, GT=13405928600en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats