Hydrogen-deuterium exchange in membrane proteins monitored by IR spectroscopy: A new tool to resolve protein structure and dynamics

As more and more high‐resolution structures of proteins become available, the new challenge is the understanding of these small conformational changes that are responsible for protein activity. Specialized difference Fourier transform infrared (FTIR) techniques allow the recording of side‐chain modi...

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Veröffentlicht in:	Biopolymers 2004-05, Vol.74 (1-2), p.19-26
Hauptverfasser:	Vigano, C., Smeyers, M., Raussens, V., Scheirlinckx, F., Ruysschaert, J.M., Goormaghtigh, E.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - chemistry Adenosine Triphosphate - chemistry amide proton attenuated total reflection Calorimetry Catalysis Cell Membrane - metabolism Deuterium Fourier transform infrared H(+)-K(+)-Exchanging ATPase - chemistry Hydrogen hydrogen deuterium exchange Kinetics membrane proteins Models, Chemical Models, Statistical Normal Distribution Phosphorylation Protein Binding Protein Conformation Protein Structure, Tertiary Protons Spectrophotometry, Infrared - methods Spectroscopy, Fourier Transform Infrared Stomach - enzymology Time Factors Water
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