File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Two-dimensional gel electrophoresis in bacterial proteomics

TitleTwo-dimensional gel electrophoresis in bacterial proteomics
Authors
KeywordsAmino acid sequence
Bacterial cell
Bacterium
Cellular distribution
Chemical labeling
Issue Date2012
PublisherSpringer and Higher Education Press. The Journal's web site is located at http://www.protein-cell.org/index.html
Citation
Protein & Cell, 2012, v. 3 n. 5, p. 346-363 How to Cite?
AbstractTwo-dimensional gel electrophoresis (2-DE) is a gel-based technique widely used for analyzing the protein composition of biological samples. It is capable of resolving complex mixtures containing more than a thousand protein components into individual protein spots through the coupling of two orthogonal biophysical separation techniques: isoelectric focusing (first dimension) and polyacrylamide gel electrophoresis (second dimension). 2-DE is ideally suited for analyzing the entire expressed protein complement of a bacterial cell: its proteome. Its relative simplicity and good reproducibility have led to 2-DE being widely used for exploring proteomics within a wide range of environmental and medically-relevant bacteria. Here we give a broad overview of the basic principles and historical development of gel-based proteomics, and how this powerful approach can be applied for studying bacterial biology and physiology. We highlight specific 2-DE applications that can be used to analyze when, where and how much proteins are expressed. The links between proteomics, genomics and mass spectrometry are discussed. We explore how proteomics involving tandem mass spectrometry can be used to analyze (post-translational) protein modifications or to identify proteins of unknown origin by de novo peptide sequencing. The use of proteome fractionation techniques and non-gel-based proteomic approaches are also discussed. We highlight how the analysis of proteins secreted by bacterial cells (secretomes or exoproteomes) can be used to study infection processes or the immune response. This review is aimed at non-specialists who wish to gain a concise, comprehensive and contemporary overview of the nature and applications of bacterial proteomics.
Persistent Identifierhttp://hdl.handle.net/10722/154730
ISSN
2023 Impact Factor: 13.6
2023 SCImago Journal Rankings: 4.412
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorCurreem, SOTen_US
dc.contributor.authorWatt, RMen_US
dc.contributor.authorLau, SKPen_US
dc.contributor.authorWoo, PCYen_US
dc.date.accessioned2012-08-08T08:27:10Z-
dc.date.available2012-08-08T08:27:10Z-
dc.date.issued2012en_US
dc.identifier.citationProtein & Cell, 2012, v. 3 n. 5, p. 346-363en_US
dc.identifier.issn1674-800Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/154730-
dc.description.abstractTwo-dimensional gel electrophoresis (2-DE) is a gel-based technique widely used for analyzing the protein composition of biological samples. It is capable of resolving complex mixtures containing more than a thousand protein components into individual protein spots through the coupling of two orthogonal biophysical separation techniques: isoelectric focusing (first dimension) and polyacrylamide gel electrophoresis (second dimension). 2-DE is ideally suited for analyzing the entire expressed protein complement of a bacterial cell: its proteome. Its relative simplicity and good reproducibility have led to 2-DE being widely used for exploring proteomics within a wide range of environmental and medically-relevant bacteria. Here we give a broad overview of the basic principles and historical development of gel-based proteomics, and how this powerful approach can be applied for studying bacterial biology and physiology. We highlight specific 2-DE applications that can be used to analyze when, where and how much proteins are expressed. The links between proteomics, genomics and mass spectrometry are discussed. We explore how proteomics involving tandem mass spectrometry can be used to analyze (post-translational) protein modifications or to identify proteins of unknown origin by de novo peptide sequencing. The use of proteome fractionation techniques and non-gel-based proteomic approaches are also discussed. We highlight how the analysis of proteins secreted by bacterial cells (secretomes or exoproteomes) can be used to study infection processes or the immune response. This review is aimed at non-specialists who wish to gain a concise, comprehensive and contemporary overview of the nature and applications of bacterial proteomics.en_US
dc.languageengen_US
dc.publisherSpringer and Higher Education Press. The Journal's web site is located at http://www.protein-cell.org/index.html-
dc.relation.ispartofProtein & Cellen_US
dc.rightsThe original publication is available at www.springerlink.com-
dc.subjectAmino acid sequenceen_US
dc.subjectBacterial cellen_US
dc.subjectBacteriumen_US
dc.subjectCellular distribution-
dc.subjectChemical labeling-
dc.titleTwo-dimensional gel electrophoresis in bacterial proteomicsen_US
dc.typeArticleen_US
dc.identifier.emailCurreem, SOT: shirly@hkucc.hku.hken_US
dc.identifier.emailWatt, RM: rmwatt@hkucc.hku.hken_US
dc.identifier.emailLau, SKP: skplau@hkucc.hku.hk-
dc.identifier.emailWoo, PCY: pcywoo@hkucc.hku.hk-
dc.identifier.authorityWatt, RM=rp00043en_US
dc.identifier.authorityWoo, PCY=rp00430en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/s13238-012-2034-5en_US
dc.identifier.pmid22610887-
dc.identifier.scopuseid_2-s2.0-84861658283en_US
dc.identifier.hkuros204357-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84861658283&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume3en_US
dc.identifier.issue5en_US
dc.identifier.spage346en_US
dc.identifier.epage363en_US
dc.identifier.isiWOS:000310528300005-
dc.publisher.placeChina-
dc.identifier.scopusauthoridWoo, PCY=7201801340en_US
dc.identifier.scopusauthoridLau, SKP=54944624200en_US
dc.identifier.scopusauthoridWatt, RM=7102907536en_US
dc.identifier.scopusauthoridCurreem, SOT=16416762100en_US
dc.identifier.issnl1674-800X-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats