From Interactions of Single Transmembrane Helices to Folding of α-Helical Membrane Proteins: Analyzing Transmembrane Helix-Helix Interactions in Bacteria

Publication type:
Journal article
Metadata:
Autoren
  • Dirk Schneider
  • Carmen Finger
  • Alexander Prodohl
  • Thomas Volkmer
DOI
10.2174/138920307779941578
ISSN
1389-2037
Ausgabe der Veröffentlichung
1
Zeitschrift
Current Protein & Peptide Science
Sprache
en
Paginierung
45 - 61
Datum der Veröffentlichung
2007
Status
Published
Herausgeber
Bentham Science Publishers Ltd.
Herausgeber URL
http://dx.doi.org/10.2174/138920307779941578
Datum der Datenerfassung
2015
Titel
From Interactions of Single Transmembrane Helices to Folding of α-Helical Membrane Proteins: Analyzing Transmembrane Helix-Helix Interactions in Bacteria
Ausgabe der Zeitschrift
8

Data source: Crossref

Other metadata sources:
Abstract
Despite a wide variety of biological functions, alpha-helical membrane proteins display a rather simple transmembrane architecture. Although not many high resolution structures of transmembrane proteins are available today, our understanding of membrane protein folding has emerged in the recent years. Now we begin to develop a basic understanding of the forces that guide folding and interaction of alpha-helical membrane proteins. Some structural requirements for transmembrane helix interactions are defined, and common motifs have been discovered in the recent years which can drive helix-helix interactions. Nevertheless, many open questions remain to be addressed in future studies. One general problem with investigating transmembrane helix interactions is the limited number of appropriate tools, which can be applied to investigate membrane protein folding. Only recently several new techniques have been developed and established, including genetic systems, which allow measuring transmembrane helix interactions in vitro and in vivo. In the first part of this review, we summarize several aspects of the current understanding of membrane protein folding and assembly. In the second part, we discuss genetic systems, which were developed in the recent years to measure interaction of transmembrane helices in the inner membrane of E. coli.
Addresses
  • Albert-Ludwigs-Universität Freiburg, Biochemie und Molekularbiologie, Stefan-Meier-Strasse 19, 79104 Freiburg, Germany. Dirk.Schneider@biochemie.uni-freiburg.de
Autoren
  • Dirk Schneider
  • Carmen Finger
  • Alexander Prodöhl
  • Thomas Volkmer
DOI
10.2174/138920307779941578
eISSN
1875-5550
Externe Identifier
  • PubMed Identifier: 17305560
Open access
false
ISSN
1389-2037
Ausgabe der Veröffentlichung
1
Zeitschrift
Current protein & peptide science
Schlüsselwörter
  • Bacterial Proteins
  • Escherichia coli Proteins
  • Membrane Proteins
  • Recombinant Fusion Proteins
  • Drug Stability
  • Signal Transduction
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Protein Folding
  • Dimerization
  • Solubility
  • Models, Molecular
Sprache
eng
Medium
Print
Paginierung
45 - 61
Datum der Veröffentlichung
2007
Status
Published
Datum der Datenerfassung
2007
Titel
From interactions of single transmembrane helices to folding of alpha-helical membrane proteins: analyzing transmembrane helix-helix interactions in bacteria.
Sub types
  • Research Support, Non-U.S. Gov't
  • Review
  • Journal Article
Ausgabe der Zeitschrift
8

Data source: Europe PubMed Central

Abstract
Despite a wide variety of biological functions, alpha-helical membrane proteins display a rather simple transmembrane architecture. Although not many high resolution structures of transmembrane proteins are available today, our understanding of membrane protein folding has emerged in the recent years. Now we begin to develop a basic understanding of the forces that guide folding and interaction of alpha-helical membrane proteins. Some structural requirements for transmembrane helix interactions are defined, and common motifs have been discovered in the recent years which can drive helix-helix interactions. Nevertheless, many open questions remain to be addressed in future studies. One general problem with investigating transmembrane helix interactions is the limited number of appropriate tools, which can be applied to investigate membrane protein folding. Only recently several new techniques have been developed and established, including genetic systems, which allow measuring transmembrane helix interactions in vitro and in vivo. In the first part of this review, we summarize several aspects of the current understanding of membrane protein folding and assembly. In the second part, we discuss genetic systems, which were developed in the recent years to measure interaction of transmembrane helices in the inner membrane of E. coli.
Autoren
  • Dirk Schneider
  • Carmen Finger
  • Alexander Prodöhl
  • Thomas Volkmer
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/17305560
DOI
10.2174/138920307779941578
ISSN
1389-2037
Ausgabe der Veröffentlichung
1
Zeitschrift
Curr Protein Pept Sci
Schlüsselwörter
  • Bacterial Proteins
  • Dimerization
  • Drug Stability
  • Escherichia coli Proteins
  • Membrane Proteins
  • Models, Molecular
  • Protein Folding
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins
  • Signal Transduction
  • Solubility
Sprache
eng
Country
United Arab Emirates
Paginierung
45 - 61
Datum der Veröffentlichung
2007
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2007
Titel
From interactions of single transmembrane helices to folding of alpha-helical membrane proteins: analyzing transmembrane helix-helix interactions in bacteria.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
  • Review
Ausgabe der Zeitschrift
8

Data source: PubMed

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