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Inter-helical Hydrogen Bond Formation During Membrane Protein Integration into the ER Membrane
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2003 In: Journal of molecular biology, ISSN 0022-2836, Vol. 334, no 4, 803-809 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2003. Vol. 334, no 4, 803-809 p.
Identifiers
URN: urn:nbn:se:su:diva-24981OAI: oai:DiVA.org:su-24981DiVA: diva2:198646
Note
Part of urn:nbn:se:su:diva-759Available from: 2005-11-23 Created: 2005-11-23Bibliographically approved
In thesis
1. Studies on the Conformation of Transmembrane Polypeptides in Membrane Proteins
Open this publication in new window or tab >>Studies on the Conformation of Transmembrane Polypeptides in Membrane Proteins
2005 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The major aim of the studies that this thesis is based on has been to better define the topological determinants of the formation of so-called helical hairpins during membrane protein assembly in the ER membrane.

The helical hairpin is a basic folding unit in membrane proteins. It is composed of two closely spaced transmembrane helices with a short connecting loop and it is believed to be inserted into the membrane as one compact unit. It is becoming increasingly clear that the helical hairpin is a very common structural element in membrane proteins and a detailed understanding of its properties is of central importance.

We demonstrate that the efficiency of formation of helical hairpins depends both on the overall length of the hydrophobic segment, on the amino acids flanking the transmembrane segment, and on the identity of the central, potentially turn-forming residues. We also show that interhelical hydrogen bonds between pairs of Asn or Asp residues can induce helical hairpin formation.

A detailed topology mapping is also reported for the Escherichia coli inner membrane chloride channel YadQ, a protein for which the X-ray structure is known. Our results provide a critical test of the reporter fusion approach and offer new insights into the YadQ folding pathway.

In summary, the results present in this thesis have increased our understanding of the determinants of membrane protein topology and structure. Furthermore, the information obtained can be used to improve current models for predictions of membrane protein topology.

Place, publisher, year, edition, pages
Stockholm: Institutionen för biokemi och biofysik, 2005. 114 p.
Keyword
membrane protein, topology, transmembrane helix, helical hairpin, turn propensity
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:su:diva-759 (URN)91-7155-175-1 (ISBN)
Public defence
2005-12-16, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 12 A, Stockholm, 14:00
Opponent
Supervisors
Available from: 2005-11-23 Created: 2005-11-23Bibliographically approved

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