Protein Flexibility and Conformational State: A Comparison of Collective Vibrational Modes of Wild-Type and D96N Bacteriorhodopsin

Far infrared (FIR) spectral measurements of wild-type (WT) and D96N mutant bacteriorhodopsin thin films have been carried out using terahertz time domain spectroscopy as a function of hydration, temperature, and conformational state. The results are compared to calculated spectra generated via norma...

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Veröffentlicht in:	Biophysical journal 2003-08, Vol.85 (2), p.1269-1277
Hauptverfasser:	Whitmire, S.E., Wolpert, D., Markelz, A.G., Hillebrecht, J.R., Galan, J., Birge, R.R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacteria Bacteriorhodopsins - chemistry Bacteriorhodopsins - radiation effects Bacteriorhodopsins - ultrastructure Computer Simulation Energy Transfer Flexibility Infrared radiation Light Models, Molecular Motion Mutation Protein Conformation - radiation effects Proteins Spectrophotometry, Infrared - methods Spectroscopy, Imaging, Other Techniques Spectrum analysis Structure-Activity Relationship Temperature Vibration Water - chemistry
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