The Stability of Transmembrane Helix Interactions Measured in a Biological Membrane

Publication type:
Journal article
Metadata:
Autoren
  • Carmen Finger
  • Thomas Volkmer
  • Alexander Prodöhl
  • Daniel E Otzen
  • Donald M Engelman
  • Dirk Schneider
DOI
10.1016/j.jmb.2006.02.065
ISSN
0022-2836
Ausgabe der Veröffentlichung
5
Zeitschrift
Journal of Molecular Biology
Sprache
en
Paginierung
1221 - 1228
Datum der Veröffentlichung
2006
Status
Published
Herausgeber
Elsevier BV
Herausgeber URL
http://dx.doi.org/10.1016/j.jmb.2006.02.065
Datum der Datenerfassung
2019
Titel
The Stability of Transmembrane Helix Interactions Measured in a Biological Membrane
Ausgabe der Zeitschrift
358

Data source: Crossref

Other metadata sources:
Abstract
Despite some promising progress in the understanding of membrane protein folding and assembly, there is little experimental information regarding the thermodynamic stability of transmembrane helix interactions and even less on the stability of transmembrane helix-helix interactions in a biological membrane. Here we describe an approach that allows quantitative measurement of transmembrane helix interactions in a biological membrane, and calculation of changes in the interaction free energy resulting from substitution of single amino acids. Dimerization of several variants of the glycophorin A transmembrane domain are characterized and compared to the wild-type (wt) glycophorin A transmembrane helix dimerization. The calculated DeltaDeltaG(app) values are further compared with values found in the literature. In addition, we compare interactions between the wt glycophorin A transmembrane domain and helices in which critical glycine residues are replaced by alanine or serine, respectively. The data demonstrate that replacement of the glycine residues by serine is less destabilizing than replacement by alanine with a DeltaDeltaG(app) value of about 0.4 kcal/mol. Our study comprises the first measurement of a transmembrane helix interaction in a biological membrane, and we are optimistic that it can be further developed and applied.
Addresses
  • Institut für Biochemie und Molekularbiologie, Albert-Ludwigs-Universität Freiburg, Stefan-Meier-Strasse 19, 79104 Freiburg, Germany.
Autoren
  • Carmen Finger
  • Thomas Volkmer
  • Alexander Prodöhl
  • Daniel E Otzen
  • Donald M Engelman
  • Dirk Schneider
DOI
10.1016/j.jmb.2006.02.065
eISSN
1089-8638
Externe Identifier
  • PubMed Identifier: 16574146
Funding acknowledgements
  • NIGMS NIH HHS: GM070985
Open access
false
ISSN
0022-2836
Ausgabe der Veröffentlichung
5
Zeitschrift
Journal of molecular biology
Schlüsselwörter
  • Escherichia coli
  • Serine Endopeptidases
  • Bacterial Proteins
  • Escherichia coli Proteins
  • Membrane Proteins
  • Recombinant Proteins
  • Amino Acid Substitution
  • Drug Stability
  • Amino Acid Sequence
  • Protein Structure, Secondary
  • Dimerization
  • Thermodynamics
Sprache
eng
Medium
Print-Electronic
Online publication date
2006
Paginierung
1221 - 1228
Datum der Veröffentlichung
2006
Status
Published
Datum der Datenerfassung
2006
Titel
The stability of transmembrane helix interactions measured in a biological membrane.
Sub types
  • Research Support, Non-U.S. Gov't
  • Journal Article
  • Research Support, N.I.H., Extramural
Ausgabe der Zeitschrift
358

Data source: Europe PubMed Central

Abstract
Despite some promising progress in the understanding of membrane protein folding and assembly, there is little experimental information regarding the thermodynamic stability of transmembrane helix interactions and even less on the stability of transmembrane helix-helix interactions in a biological membrane. Here we describe an approach that allows quantitative measurement of transmembrane helix interactions in a biological membrane, and calculation of changes in the interaction free energy resulting from substitution of single amino acids. Dimerization of several variants of the glycophorin A transmembrane domain are characterized and compared to the wild-type (wt) glycophorin A transmembrane helix dimerization. The calculated DeltaDeltaG(app) values are further compared with values found in the literature. In addition, we compare interactions between the wt glycophorin A transmembrane domain and helices in which critical glycine residues are replaced by alanine or serine, respectively. The data demonstrate that replacement of the glycine residues by serine is less destabilizing than replacement by alanine with a DeltaDeltaG(app) value of about 0.4 kcal/mol. Our study comprises the first measurement of a transmembrane helix interaction in a biological membrane, and we are optimistic that it can be further developed and applied.
Date of acceptance
2006
Autoren
  • Carmen Finger
  • Thomas Volkmer
  • Alexander Prodöhl
  • Daniel E Otzen
  • Donald M Engelman
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/16574146
DOI
10.1016/j.jmb.2006.02.065
Funding acknowledgements
  • NIGMS NIH HHS: GM070985
ISSN
0022-2836
Ausgabe der Veröffentlichung
5
Zeitschrift
J Mol Biol
Schlüsselwörter
  • Amino Acid Sequence
  • Amino Acid Substitution
  • Bacterial Proteins
  • Dimerization
  • Drug Stability
  • Escherichia coli
  • Escherichia coli Proteins
  • Membrane Proteins
  • Protein Structure, Secondary
  • Recombinant Proteins
  • Serine Endopeptidases
  • Thermodynamics
Sprache
eng
Country
Netherlands
Paginierung
1221 - 1228
PII
S0022-2836(06)00281-6
Datum der Veröffentlichung
2006
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2006
Titel
The stability of transmembrane helix interactions measured in a biological membrane.
Sub types
  • Journal Article
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
Ausgabe der Zeitschrift
358

Data source: PubMed

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