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The role of the surface group in funnelling of protons towards the protonic channel of bacteriorhodopsin

โœ Scribed by Esther Nachliel; Sharon Yaniv-Checover; Menahem Gutman


Publisher
Elsevier Science
Year
1997
Tongue
English
Weight
809 KB
Volume
97
Category
Article
ISSN
0167-2738

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โœฆ Synopsis


The dynamics of proton transfer between the bulk and an indicator attached to a defined site on a protein (bacteriorhodopsin) was measured in the time resolved domain. The labelling was attached to the cytoplasmic surface of the protein at the opening of its proton conducting channel (residue 38). Detailed analysis of the results indicates that a nearby carboxylate (aspartate 36) functions as a relay group that accelerates the entrance of proton to the channel. A farther located cluster, of 3 carboxylates, also functions in the same mode. These observations indicate that the surface of the protein had evolved as a functional element in directing the substrate towards the active site.


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The role of aromatic groups in the Tobey
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## Abstract The Tobeyโ€“Simon (additivity) rule for aromatic groups which was devised about 40 years ago has been found to need revision. The rule shows an aromatic group attached to a C๏ฃพC double bond as causing a downfield chemical shift of a __cis__โ€related vinylic proton and a small upfield shift