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Spin Labeling Studies of Transmembrane Signaling and Transport: Applications to Phototaxis, ABC Transporters and Symporters.
- Source :
-
Methods in enzymology [Methods Enzymol] 2015; Vol. 564, pp. 315-47. Date of Electronic Publication: 2015 Jun 23. - Publication Year :
- 2015
-
Abstract
- Membrane proteins still represent a major challenge for structural biologists. This chapter will focus on the application of continuous wave and pulsed EPR spectroscopy on spin-labeled membrane proteins. Site-directed spin labeling EPR spectroscopy has evolved as a powerful tool to study the structure and dynamics of proteins, especially membrane proteins, as this method works largely independently of the size and complexity of the biological system under investigation. This chapter describes applications of this technique to three different systems: the archaeal photoreceptor/-transducer complex SRII/HtrII as an example for transmembrane signaling and two transport systems, the histidine ATP-binding cassette transporter HisQMP, and the sodium-proline symporter PutP.<br /> (© 2015 Elsevier Inc. All rights reserved.)
- Subjects :
- ATP-Binding Cassette Transporters chemistry
Amino Acid Transport Systems, Neutral chemistry
Archaea chemistry
Archaea cytology
Archaeal Proteins chemistry
Bacterial Proteins chemistry
Biological Transport
Cell Movement
Electron Spin Resonance Spectroscopy methods
Escherichia coli chemistry
Escherichia coli cytology
Escherichia coli Proteins chemistry
Light
Models, Molecular
Protein Conformation
Salmonella typhimurium chemistry
Salmonella typhimurium cytology
Signal Transduction
Spin Labels
Symporters chemistry
ATP-Binding Cassette Transporters metabolism
Amino Acid Transport Systems, Neutral metabolism
Archaea metabolism
Archaeal Proteins metabolism
Bacterial Proteins metabolism
Escherichia coli metabolism
Escherichia coli Proteins metabolism
Salmonella typhimurium metabolism
Symporters metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1557-7988
- Volume :
- 564
- Database :
- MEDLINE
- Journal :
- Methods in enzymology
- Publication Type :
- Academic Journal
- Accession number :
- 26477256
- Full Text :
- https://doi.org/10.1016/bs.mie.2015.05.025