Retinal Schiff bases with aromatic and aliphatic amino acids — the extremely different nature of the intramolecular hydrogen bond between the two types of compounds
暂无分享,去创建一个
[1] H. Khorana,et al. Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that ASP-96 deprotonates during the M----N transition. , 1991, The Journal of biological chemistry.
[2] J. Olejnik,et al. Phenol—retinal schiff base hydrogen bonds—influence of steric hindrance and phenol acidity on the thermodynamic data of formation and proton transfer , 1990 .
[3] E. Bamberg,et al. Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump. , 1989, The EMBO journal.
[4] G. Zundel,et al. Influence of phenol acidity and solvent polarity with phenol—retinal schiff base hydrogen bonds—thermodynamic parameters of bond formation and proton transfer , 1987 .
[5] G. Zundel,et al. Thermodynamics of proton transfer in carboxylic acid-retinal Schiff base hydrogen bonds with large proton polarizability. , 1986, Biochemical and biophysical research communications.