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BIOspektrum

, Volume 21, Issue 7, pp 718–720 | Cite as

Proteinvermessung: Präzise Abstandsverteilungen im Nanometerbereich

  • Julia Cattani
  • Marta Robotta
  • Malte DrescherEmail author
Wissenschaft · Methoden Struktur und Dynamik von Biomakromolekülen
  • 70 Downloads

Abstract

Long range distance constraints are crucial for investigating structure and dynamics of bio-macromolecules. Exploiting electron paramagnetic resonance spectroscopy in combination with site-directed spin labelling gives access to precise distance distributions in the nanometer range, even for large protein complexes and in complex environments, e. g., in cellula.

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Literatur

  1. [1]
    Heyduk T (2002) Measuring protein conformational changes by FRET/LRET. Curr Opin Biotechnol 13:292–296CrossRefPubMedGoogle Scholar
  2. [2]
    Hubbell WL, Altenbach C (1994) Site-Directed Spin Labeling of Membrane Proteins. In: White SH (Hrsg) Membrane Protein Structure. Springer, New York, S 224–248CrossRefGoogle Scholar
  3. [3]
    Likhtenshtein GI, Yamauchi J, Nakatsuji S et al. (2008) Nitroxides: Applications in Chemistry, Biomedicine, and Materials Science. John Wiley & Sons, WeinheimCrossRefGoogle Scholar
  4. [4]
    Schmidt MJ, Borbas J, Drescher M et al. (2014) A genetically encoded spin label for electron paramagnetic resonance distance measurements. J Am Chem Soc 136:1238–1241CrossRefPubMedGoogle Scholar
  5. [5]
    Klare JP, Steinhoff H-J (2009) Spin labeling EPR. Photosynth Res 102:377–390CrossRefPubMedGoogle Scholar
  6. [6]
    Jeschke G (2012) DEER distance measurements on proteins. Annu Rev Phys Chem 63:419–446CrossRefPubMedGoogle Scholar
  7. [7]
    Robotta M, Gerding HR, Vogel A et al. (2014) Alpha- Synuclein binds to the inner membrane of mitochondria in an a-helical conformation. Chembiochem 15:2499–2502CrossRefPubMedGoogle Scholar
  8. [8]
    Azarkh M, Singh V, Okle O et al. (2013) Site-directed spinlabeling of nucleotides and the use of in-cell EPR to determine long-range distances in a biologically relevant environment. Nat Protoc 8:131–147CrossRefPubMedGoogle Scholar
  9. [9]
    Qi M, Groß A, Jeschke G et al. (2014) Gd(III)-PyMTA label is suitable for in-cell EPR. J Am Chem Soc 136:15366–15378CrossRefPubMedGoogle Scholar
  10. [10]
    Hänsel R, Luh LM, Corbeski I et al. (2014) In-cell NMR and EPR spectroscopy of biomacromolecules. Angew Chem Int Ed 53:10300–10314CrossRefGoogle Scholar
  11. [11]
    Robotta M, Braun P, van Rooijen B et al. (2011) Direct evidence of coexisting horseshoe and extended helix conformations of membrane-bound alpha-synuclein. Chemphyschem 12:267–269CrossRefPubMedGoogle Scholar
  12. [12]
    Drescher M, Huber M, Subramaniam V (2012) Hunting the chameleon: structural conformations of the intrinsically disordered protein alpha-synuclein. Chembiochem 13:761–768CrossRefPubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Fachbereich ChemieUniversität KonstanzKonstanzDeutschland

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