Photo-Crosslinking Analysis of Preferential Interactions between a Transmembrane Peptide and Matching Lipids

In this study, a novel method is presented by which the molecular environment of a transmembrane peptide can be investigated directly. This was achieved by incorporating a photoactivatable crosslinking probe in the hydrophobic segment of a model transmembrane peptide. When this peptide was incorpora...

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Veröffentlicht in:	Biochemistry (Easton) 2004-04, Vol.43 (15), p.4482-4489
Hauptverfasser:	Ridder, Anja N. J. A, Spelbrink, Robin E. J, Demmers, Jeroen A. A, Rijkers, Dirk T. S, Liskamp, Rob M. J, Brunner, Josef, Heck, Albert J. R, de Kruijff, Ben, Killian, J. Antoinette
Format:	Artikel
Sprache:	eng
Schlagworte:	1,2-Dipalmitoylphosphatidylcholine - chemistry Amino Acid Sequence Azirines - metabolism Cross-Linking Reagents - metabolism Dimyristoylphosphatidylcholine - chemistry Hydrophobic and Hydrophilic Interactions Lipid Bilayers - chemistry Lipid Bilayers - metabolism Membrane Proteins - chemical synthesis Membrane Proteins - metabolism Molecular Sequence Data Peptides - chemical synthesis Peptides - metabolism Phenylalanine - analogs & derivatives Photoaffinity Labels - metabolism Photochemistry Spectrometry, Mass, Electrospray Ionization Ultraviolet Rays
Online-Zugang:	Volltext
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