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Pàgina inicial > Articles > Articles publicats > Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach |
Data: | 2012 |
Resum: | Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C13 of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoproteins with all-trans-retinal and its 20-methyl derivative (hereafter, 13-ethyl retinal). Biophysical characterization indicates that recovering the steric interaction between the residue 90 and retinal, eases the accommodation of the chromophore, however it is not enough for a complete phenotype rescue. The characterization of these chemically engineered chromoproteins provides further insight into the role of the hydrogen bond network and the steric interactions involving the retinal binding pocket in bacteriorhodopsin and other microbial sensory rhodopsins. |
Ajuts: | European Commission 237120 Ministerio de Ciencia e Innovación BES-2004-5542 Ministerio de Ciencia e Innovación BFU2009-08758 Ministerio de Ciencia e Innovación SAF2010-21385 Ministerio de Ciencia e Innovación SAF2010-17935 |
Drets: | Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original. |
Llengua: | Anglès |
Document: | Article ; Versió publicada |
Matèria: | Protons ; Thermal stability ; Hydrogen bonding ; Chromoproteins ; Phosphates ; Ultraviolet-visible spectroscopy |
Publicat a: | PloS one, Vol. 7, Issue 8 (August 2012) , p. e42447, ISSN 1932-6203 |
9 p, 1.3 MB |