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 Photobioljournal_title
Photochemistry and photobiologyauthors
Sekharan Sdoi
10.1111/j.1751-1097.2008.00499.xsubject
Has Abstractpub_date
2009-03-01 00:00:00pages
517-20issue
2eissn
0031-8655issn
1751-1097pii
PHP499journal_volume
85pub_type
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