Book chapter
English

Site-Directed Spin Labeling of Membrane Proteins

Contributors

Bordignon, Enrica

Publisher

Springer

Collection

  • Topics in current chemistry; 321

Publication date

2011-09-07

First online date

2011-09-07

Abstract

EPR spectroscopy of site-directed spin labeled membrane proteins is at present a common and valuable biophysical tool to study structural details and conformational transitions under conditions relevant to function. EPR is considered a complementary approach to X-ray crystallography and NMR because it provides detailed information on (1) side chain dynamics with an exquisite sensitivity for flexible regions, (2) polarity and water accessibility profiles across the membrane bilayer, and (3) distances between two spin labeled side chains during protein functioning. Despite the drawback of requiring site-directed mutagenesis for each new piece of information to be collected, EPR can be applied to any complex membrane protein system, independently of its size. This chapter describes the state of the art in the application of site-directed spin labeling (SDSL) EPR to membrane proteins, with specific focus on the different types of information which can be obtained with continuous wave and pulsed techniques.

Keywords

  • Conformational changes
  • Distances
  • Dynamics
  • EPR
  • Membrane proteins
  • Spin labeling
  • Structural biology
  • Water accessibility

UNIGE affiliation entities

Not a UNIGE publication

Citation (ISO format)

BORDIGNON, Enrica. Site-Directed Spin Labeling of Membrane Proteins. In: EPR Spectroscopy : Applications in Chemistry and Biology. [s.l.] : Springer, 2011. p. 121–157. (Topics in current chemistry) doi: 10.1007/128_2011_243

Main files (1)

Book chapter (Published version)

Identifiers

Additional URL for this publication

https://link.springer.com/10.1007/128_2011_243

ISBN

978-3-642-28346-8
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Technical informations

Creation

05/12/2023 18:33:14

First validation

06/12/2023 12:56:22

Update

06/12/2023 12:56:22

Status update

06/12/2023 12:56:22

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