Proteomic analysis of heat-stable proteins in Escherichia coli
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kwon, Soonbok | - |
dc.contributor.author | Jung, Yuna | - |
dc.contributor.author | Lim, Dongbin | - |
dc.date.available | 2018-05-10T16:01:54Z | - |
dc.date.created | 2018-04-17 | - |
dc.date.issued | 2008-02-29 | - |
dc.identifier.issn | 1976-6696 | - |
dc.identifier.uri | http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/16902 | - |
dc.description.abstract | Some proteins of E coli are stable at temperatures significantly higher than 49 degrees C, the maximum temperature at which the organism can grow. The heat stability of such proteins would be a property which is inherent to their structures, or it might be acquired by evolution for their specialized functions. In this study, we describe the identification of 17 heat-stable proteins from E coli. Approximately one-third of these proteins were recognized as having functions in the protection of other proteins against denaturation. These included chaperonin (GmEL and GroES), molecular chaperones (DnaK and FkpA) and peptidyl prolyl isomerases (trigger factor and FkpA). Another common feature was that five of these proteins (GroEL, GroES, Ahpc, RibH and ferritin) have been shown to form a macromolecular structure. These results indicated that the heat stability of certain proteins may have evolved for their specialized functions, allowing them to cope with harsh environments, including high temperatures. | - |
dc.publisher | KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY | - |
dc.relation.isPartOf | BMB REPORTS | - |
dc.subject | CHAPERONIN GROEL | - |
dc.subject | IDENTIFICATION | - |
dc.subject | PURIFICATION | - |
dc.subject | ENOLASE | - |
dc.subject | GROWTH | - |
dc.subject | RNA | - |
dc.title | Proteomic analysis of heat-stable proteins in Escherichia coli | - |
dc.type | Article | - |
dc.identifier.doi | 10.5483/BMBRep.2008.41.2.108 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | BMB REPORTS, v.41, no.2, pp.108 - 111 | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000255359500003 | - |
dc.citation.endPage | 111 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 108 | - |
dc.citation.title | BMB REPORTS | - |
dc.citation.volume | 41 | - |
dc.contributor.affiliatedAuthor | Lim, Dongbin | - |
dc.type.docType | Article | - |
dc.description.oadoiVersion | published | - |
dc.subject.keywordAuthor | E. coli | - |
dc.subject.keywordAuthor | heat stability | - |
dc.subject.keywordAuthor | heat treatment | - |
dc.subject.keywordAuthor | proteomics | - |
dc.subject.keywordAuthor | thermostable | - |
dc.subject.keywordPlus | CHAPERONIN GROEL | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | ENOLASE | - |
dc.subject.keywordPlus | GROWTH | - |
dc.subject.keywordPlus | RNA | - |
dc.description.journalRegisteredClass | scopus | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
Soongsil University Library 369 Sangdo-Ro, Dongjak-Gu, Seoul, Korea (06978)02-820-0733
COPYRIGHT ⓒ SOONGSIL UNIVERSITY, ALL RIGHTS RESERVED.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.