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- PMID: 16190669
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Article: Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by fourier transform infrared spectroscopy and differential scanning calorimetry
Title | Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by fourier transform infrared spectroscopy and differential scanning calorimetry |
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Authors | |
Keywords | Aggregation Buckwheat globulin Denaturation Differential scanning calorimetry Fagopyrum esculentum Moench FTIR spectroscopy Protein conformation |
Issue Date | 2005 |
Publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau |
Citation | Journal Of Agricultural And Food Chemistry, 2005, v. 53 n. 20, p. 8046-8053 How to Cite? |
Abstract | Fourier transform infrared (FTIR) spectroscopy and differential scanning calorimetry (DSC) were used to study changes in the conformation of globulin from common buckwheat (Fagopyrum esculentum Moench) (BWG) under various environmental conditions. The IR spectrum of the native BWG showed several major bands from 1691 to 1636 cm -1 in the amide I′ region, and the secondary structure composition was estimated as 34.5% β-sheets, 20.0% β-turns, 16.0% α-helices, and 14.4% random coils. Highly acidic and alkaline pH conditions induced decreases in β-sheet and α-helical contents, as well as in denaturation temperature (T d) and enthalpy of denaturation (ΔH), as shown in the DSC thermograms. Addition of chaotropic salts (1.0 M) caused progressive decreases in ordered structures and thermal stability following the lyotropic series of anions. The presence of several protein structure perturbants also led to changes in IR band intensities and DSC thermal stabilities, suggesting protein unfolding. Intermolecular antiparallel β-sheet (1620 and 1681 cm -1) band intensities started to increase when BWG was heated to 90°C, suggesting the initiation of protein aggregation. Increasing the time of the preheat treatment (at 100°C) caused progressive increases in T d and pronounced decreases in ΔH, suggesting partial denaturation and reassociation of protein molecules. © 2005 American Chemical Society. |
Persistent Identifier | http://hdl.handle.net/10722/68521 |
ISSN | 2023 Impact Factor: 5.7 2023 SCImago Journal Rankings: 1.114 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
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dc.contributor.author | Choi, SM | en_HK |
dc.contributor.author | Ma, CY | en_HK |
dc.date.accessioned | 2010-09-06T06:05:20Z | - |
dc.date.available | 2010-09-06T06:05:20Z | - |
dc.date.issued | 2005 | en_HK |
dc.identifier.citation | Journal Of Agricultural And Food Chemistry, 2005, v. 53 n. 20, p. 8046-8053 | en_HK |
dc.identifier.issn | 0021-8561 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/68521 | - |
dc.description.abstract | Fourier transform infrared (FTIR) spectroscopy and differential scanning calorimetry (DSC) were used to study changes in the conformation of globulin from common buckwheat (Fagopyrum esculentum Moench) (BWG) under various environmental conditions. The IR spectrum of the native BWG showed several major bands from 1691 to 1636 cm -1 in the amide I′ region, and the secondary structure composition was estimated as 34.5% β-sheets, 20.0% β-turns, 16.0% α-helices, and 14.4% random coils. Highly acidic and alkaline pH conditions induced decreases in β-sheet and α-helical contents, as well as in denaturation temperature (T d) and enthalpy of denaturation (ΔH), as shown in the DSC thermograms. Addition of chaotropic salts (1.0 M) caused progressive decreases in ordered structures and thermal stability following the lyotropic series of anions. The presence of several protein structure perturbants also led to changes in IR band intensities and DSC thermal stabilities, suggesting protein unfolding. Intermolecular antiparallel β-sheet (1620 and 1681 cm -1) band intensities started to increase when BWG was heated to 90°C, suggesting the initiation of protein aggregation. Increasing the time of the preheat treatment (at 100°C) caused progressive increases in T d and pronounced decreases in ΔH, suggesting partial denaturation and reassociation of protein molecules. © 2005 American Chemical Society. | en_HK |
dc.language | eng | en_HK |
dc.publisher | American Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau | en_HK |
dc.relation.ispartof | Journal of Agricultural and Food Chemistry | en_HK |
dc.subject | Aggregation | en_HK |
dc.subject | Buckwheat globulin | en_HK |
dc.subject | Denaturation | en_HK |
dc.subject | Differential scanning calorimetry | en_HK |
dc.subject | Fagopyrum esculentum Moench | en_HK |
dc.subject | FTIR spectroscopy | en_HK |
dc.subject | Protein conformation | en_HK |
dc.title | Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by fourier transform infrared spectroscopy and differential scanning calorimetry | en_HK |
dc.type | Article | en_HK |
dc.identifier.openurl | http://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-8561&volume=53&spage=8046&epage=8053&date=2005&atitle=Conformational+study+of+globulin+from+common+buckwheat+(Fagopyrum+esculentum+Moench)+by+Fourier+transform+infrared+spectroscopy+and+differential+scanning+calorimetry | en_HK |
dc.identifier.email | Ma, CY: macy@hkucc.hku.hk | en_HK |
dc.identifier.authority | Ma, CY=rp00759 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1021/jf051040v | en_HK |
dc.identifier.pmid | 16190669 | - |
dc.identifier.scopus | eid_2-s2.0-27144501099 | en_HK |
dc.identifier.hkuros | 115291 | en_HK |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-27144501099&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 53 | en_HK |
dc.identifier.issue | 20 | en_HK |
dc.identifier.spage | 8046 | en_HK |
dc.identifier.epage | 8053 | en_HK |
dc.identifier.isi | WOS:000232288800061 | - |
dc.publisher.place | United States | en_HK |
dc.identifier.scopusauthorid | Choi, SM=8873744400 | en_HK |
dc.identifier.scopusauthorid | Ma, CY=7402924944 | en_HK |
dc.identifier.issnl | 0021-8561 | - |