Membrane orientation of the N-terminal segment of alamethicin determined by solid-state 15N NMR.

Lignende værker

• Structure and Alignment of the Membrane-Associated Peptaibols Ampullosporin A and Alamethicin by Oriented (15)N and (31)P Solid-State NMR Spectroscopy
  af: Salnikov, Evgeniy S., et al.
  Udgivet: (2009)
• Collisions between helical peptides in membranes monitored using electron paramagnetic resonance: evidence that alamethicin is monomeric in the absence of a membrane potential.
  af: Barranger-Mathys, M, et al.
  Udgivet: (1994)
• Conformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance.
  af: Bak, M, et al.
  Udgivet: (2001)
• Membrane insertion and orientation of polyalanine peptides: a (15)N solid-state NMR spectroscopy investigation.
  af: Bechinger, B
  Udgivet: (2001)
• Helix Conformations in 7TM Membrane Proteins Determined Using Oriented-Sample Solid-State NMR with Multiple Residue-Specific (15)N Labeling
  af: Vosegaard, Thomas, et al.
  Udgivet: (2008)