Folding energetics and oligomerization of polytopic α-helical transmembrane proteins

Publication type:
Journal article
Metadata:
Autoren
  • Jennifer Neumann
  • Noreen Klein
  • Daniel E Otzen
  • Dirk Schneider
DOI
10.1016/j.abb.2014.07.017
ISSN
0003-9861
Zeitschrift
Archives of Biochemistry and Biophysics
Sprache
en
Paginierung
281 - 296
Datum der Veröffentlichung
2014
Status
Published
Herausgeber
Elsevier BV
Herausgeber URL
http://dx.doi.org/10.1016/j.abb.2014.07.017
Datum der Datenerfassung
2021
Titel
Folding energetics and oligomerization of polytopic α-helical transmembrane proteins
Ausgabe der Zeitschrift
564

Data source: Crossref

Other metadata sources:
Abstract
While interactions of single-span transmembrane helices have been studied to a significant extent in the past years, the folding of polytopic α-helical transmembrane proteins, as well as their oligomerization, are far less analyzed and understood. The goal of the few thus far performed thermodynamic studies, in which unfolding of polytopic TM proteins was described, was to achieve a mild, potentially reversible unfolding process, to finally derive thermodynamic parameters for the reverse folding pathway. In the first part of this review, we summarize the studies analyzing the thermodynamic stability and folding pathways of polytopic transmembrane proteins. Based on these studies, we deduce some common principles, guiding transmembrane protein unfolding and folding, important for the design of future folding/unfolding studies. Furthermore, the discussed observations can conceptually guide an experimental search for proper in vitro transmembrane protein refolding conditions. In many of the resolved membrane protein structures, individual monomers interact to form higher ordered oligomers. In most cases, oligomerization of those monomeric units appears to be intimately linked to the protein function, and folding of the individual protomers might even occur only after interaction. In the second part of this review, we discuss folding pathways of oligomeric α-helical transmembrane proteins as well as causes and consequences of α-helical transmembrane protein oligomerization.
Addresses
  • Department of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, 55128 Mainz, Germany.
Autoren
  • Jennifer Neumann
  • Noreen Klein
  • Daniel E Otzen
  • Dirk Schneider
DOI
10.1016/j.abb.2014.07.017
eISSN
1096-0384
Externe Identifier
  • PubMed Identifier: 25057769
Funding acknowledgements
  • German Chemical Industry Fund:
  • Stiftung Rheinland-Pfalz für Innovation:
  • Danish Research Foundation:
  • Danish Research Council|Natural Sciences:
  • Deutsche Forschungsgemeinschaft:
Open access
false
ISSN
0003-9861
Zeitschrift
Archives of biochemistry and biophysics
Schlüsselwörter
  • Cell Membrane
  • Animals
  • Humans
  • Membrane Proteins
  • Protein Structure, Secondary
  • Protein Folding
  • Protein Multimerization
Sprache
eng
Medium
Print-Electronic
Online publication date
2014
Paginierung
281 - 296
Datum der Veröffentlichung
2014
Status
Published
Datum der Datenerfassung
2014
Titel
Folding energetics and oligomerization of polytopic α-helical transmembrane proteins.
Sub types
  • Research Support, Non-U.S. Gov't
  • Review
  • Journal Article
Ausgabe der Zeitschrift
564

Data source: Europe PubMed Central

Abstract
While interactions of single-span transmembrane helices have been studied to a significant extent in the past years, the folding of polytopic α-helical transmembrane proteins, as well as their oligomerization, are far less analyzed and understood. The goal of the few thus far performed thermodynamic studies, in which unfolding of polytopic TM proteins was described, was to achieve a mild, potentially reversible unfolding process, to finally derive thermodynamic parameters for the reverse folding pathway. In the first part of this review, we summarize the studies analyzing the thermodynamic stability and folding pathways of polytopic transmembrane proteins. Based on these studies, we deduce some common principles, guiding transmembrane protein unfolding and folding, important for the design of future folding/unfolding studies. Furthermore, the discussed observations can conceptually guide an experimental search for proper in vitro transmembrane protein refolding conditions. In many of the resolved membrane protein structures, individual monomers interact to form higher ordered oligomers. In most cases, oligomerization of those monomeric units appears to be intimately linked to the protein function, and folding of the individual protomers might even occur only after interaction. In the second part of this review, we discuss folding pathways of oligomeric α-helical transmembrane proteins as well as causes and consequences of α-helical transmembrane protein oligomerization.
Date of acceptance
2014
Autoren
  • Jennifer Neumann
  • Noreen Klein
  • Daniel E Otzen
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/25057769
DOI
10.1016/j.abb.2014.07.017
eISSN
1096-0384
Zeitschrift
Arch Biochem Biophys
Schlüsselwörter
  • Folding energetics
  • Membrane protein
  • Oligomerization
  • Protein folding
  • Animals
  • Cell Membrane
  • Humans
  • Membrane Proteins
  • Protein Folding
  • Protein Multimerization
  • Protein Structure, Secondary
Sprache
eng
Country
United States
Paginierung
281 - 296
PII
S0003-9861(14)00268-9
Datum der Veröffentlichung
2014
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2015
Titel
Folding energetics and oligomerization of polytopic α-helical transmembrane proteins.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
  • Review
Ausgabe der Zeitschrift
564

Data source: PubMed

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