Amino Acids

Posted June 25th, 2016 by Tony. Comments Off on Amino Acids.

The subsequent transfer mechanism proton through bacteriorhodopsin involves a chain of hydrogen bonds formed by amino acid side radicals of hydrophilic and extends through the entire thickness of the protein. Proton transfer through the chain can be carried out in if it consists of two parts and contains a functional group capable of change when exposed to light their microenvironment and thereby consistently "close" and "unlock" these areas. The role of the "Shuttle" mechanism between the two conductors of the protein protons, one of which communicates with the external and the other – with the cytoplasmic surface of the cell membrane, plays in retinal aldimin residue lysine-216. Mechanism of the "proton pump" bacteriorhodopsin studied intensively in many laboratories around the world. This unusual protein remains the focus of researchers for several reasons. First of all, thanks to its high sensitivity and resolution, it is widely used in applications such as natural photochromic material 2. In addition, bacteriorhodopsin is very attractive as a model for studies related to the study of functional activity and structural properties of membrane proteins in the native energopreobrazuyuschih membranes. For detailed information about the structure of the polypeptide chain of the membrane protein in the native membrane is selectively useful to introduce the isotopic label the protein's ability to use spectral methods for high resolution, such as nuclear magnetic resonance spectroscopy (NMR) 3, Raman and laser spectroscopy 4,5, infrared (IR) spectroscopy 6 and mass spectrometry (MS) 7. In this regard, especially prospective studies with bacteriorhodopsin, selectively enriched stable isotopes, such as deuterium on the balance of functionally important amino acids such as L-phenylalanine, L-tyrosine and L-tryptophan 8,9.

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