The synergetic effects of combining structural biology and epr spectroscopy on membrane proteins

  • Protein structures as provided by structural biology such as X-ray crystallography, cryo-electron microscopy and NMR spectroscopy are key elements to understand the function of a protein on the molecular level. Nonetheless, they might be error-prone due to crystallization artifacts or, in particular in case of membrane-imbedded proteins, a mostly artificial environment. In this review, we will introduce different EPR spectroscopy methods as powerful tools to complement and validate structural data gaining insights in the dynamics of proteins and protein complexes such that functional cycles can be derived. We will highlight the use of EPR spectroscopy on membrane-embedded proteins and protein complexes ranging from receptors to secondary active transporters as structural information is still limited in this field and the lipid environment is a particular challenge.

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Author:Dorith Wunnicke, Inga Hänelt
URN:urn:nbn:de:hebis:30:3-514656
DOI:https://doi.org/10.3390/cryst7040117
ISSN:2073-4352
Parent Title (English):Crystals
Publisher:MDPI
Place of publication:Basel
Contributor(s):Albert Guskov
Document Type:Article
Language:English
Year of Completion:2017
Date of first Publication:2017/04/20
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2019/10/23
Tag:EPR spectroscopy; PELDOR; membrane proteins; structural biology
Volume:7
Issue:4, Art. 117
Page Number:29
First Page:1
Last Page:29
Note:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited
HeBIS-PPN:455918031
Institutes:Biochemie, Chemie und Pharmazie / Biochemie und Chemie
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - Namensnennung 4.0