Title of article :
Hydrogen-deuterium exchange in membrane proteins monitored by IR spectroscopy: A new tool to resolve protein structure and dynamics
Author/Authors :
Vigano، C. نويسنده , , Smeyers، M. نويسنده , , Raussens، V. نويسنده , , Scheirlinckx، F. نويسنده , , Ruysschaert، J.M. نويسنده , , Goormaghtigh، E. نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2004
Pages :
-18
From page :
19
To page :
0
Abstract :
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 modifications or minute secondary structure changes. Yet, large domain movements remain usually unnoticed. FTIR spectroscopy provides a unique opportunity to record 1H/2H exchange kinetics at the level of the amide proton. This approach is extremely sensitive to tertiary structure changes and yields quantitative data on domain/domain interactions. An experimental setup designed for attenuated total reflection and a specific approach for the analysis of the results is described. The study of one membrane protein, the gastric H^+,K^+-ATPase, demonstrates the usefulness of 1H/2H exchange kinetics for the understanding of the molecular movement related to the catalytic activity.
Keywords :
hydrogen deuterium exchange , membrane proteins , Fourier transform infrared , Attenuated total reflection , amide proton
Journal title :
BIOPOLYMERS (ORIGINAL RESEARCH ON BIOMOLECULES)
Serial Year :
2004
Journal title :
BIOPOLYMERS (ORIGINAL RESEARCH ON BIOMOLECULES)
Record number :
120807
Link To Document :
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