Water-mediated spectral shifts in rhodopsin and bathorhodopsin.

Abstract:

:The role of water molecules in spectral tuning of proteins has been left largely unexplored. This topic is important because changing hydrogen bond patterns during the activation process may lead to spectral shifts which can be of diagnostic value for the underlying structures. Arguments put forward in this article are based on spectral shift calculations of the rhodopsin and bathorhodopsin chromophore due to wat2a and 2b in the presence and absence of the counterion and of the amino acids lining the rhodopsin binding pocket. They show, among others, that a single water molecule can shift the absorbance by up to 0.1 eV or 34 nm depending on the environment of the chromophore.

journal_name

Photochem Photobiol

authors

Sekharan S

doi

10.1111/j.1751-1097.2008.00499.x

subject

Has Abstract

pub_date

2009-03-01 00:00:00

pages

517-20

issue

2

eissn

0031-8655

issn

1751-1097

pii

PHP499

journal_volume

85

pub_type

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