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• W2047713089 abstract "Time-resolved Fourier transform infrared (FTIR) difference spectroscopy is a valuable tool for monitoring the dynamics of protein reactions and interactions. Absorbance changes can be monitored with time resolutions down to nanoseconds and followed for time periods that range over nine orders of magnitude. Membrane proteins bound to solid supported lipid bilayers can be investigated in near physiological conditions with the attenuated total reflection (ATR) technique. Here, we review the basics of time-resolved FTIR with a focus on Ras, a GTPase that is mutated in 25% of human tumors. We show the first time-resolved measurements of membrane anchored Ras and observed the switching between its activated and its inactivated state. We compared those measurements with measurements of the truncated Ras in solution. We found that both the kinetics and the functional groups involved were very similar. This suggested that the membrane did not have a major influence on the hydrolysis reaction." @default.
• W2047713089 created "2016-06-24" @default.
• W2047713089 creator A5025739247 @default.
• W2047713089 creator A5061965371 @default.
• W2047713089 creator A5080182543 @default.
• W2047713089 date "2012-03-01" @default.
• W2047713089 modified "2023-10-14" @default.
• W2047713089 title "Time-resolved FTIR spectroscopy for monitoring protein dynamics exemplified by functional studies of Ras protein bound to a lipid bilayer" @default.
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• W2047713089 doi "https://doi.org/10.1016/j.chemphys.2011.08.007" @default.
• W2047713089 hasPublicationYear "2012" @default.
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