Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that Thr-46 and Thr-89 form part of a transient network of hydrogen bonds

The role of Thr-46 and Thr-89 in the bacteriorhodopsin photocycle has been investigated by Fourier transform infrared difference spectroscopy and time-resolved visible absorption spectroscopy of site-directed mutants. Substitutions of Thr-46 and Thr-89 reveal alterations in the chromophore and prote...

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Veröffentlicht in:	The Journal of biological chemistry 1992-01, Vol.267 (3), p.1615-1622
Hauptverfasser:	Rothschild, K J, He, Y W, Sonar, S, Marti, T, Khorana, H G
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry bacteriorhodopsin Bacteriorhodopsins - chemistry Bacteriorhodopsins - genetics Biological and medical sciences Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Hydrogen Bonding Mutagenesis, Site-Directed Non metallic chromoproteins, photoproteins Protein Conformation Proteins Spectrophotometry, Infrared Thermodynamics Threonine Vibration
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