Conformationally averaged score functions for electronic propagation in proteins.
J Phys Chem B
; 110(11): 5747-57, 2006 Mar 23.
Article
in En
| MEDLINE
| ID: mdl-16539520
ABSTRACT
We explore the influence of conformational dynamics on protein-mediated electron donor-acceptor interactions. We introduce a thermally averaged score function to characterize electronic propagation from redox cofactors into the protein and solvent. The score function is explored for myoglobin at the extended-Hückel level, and the results are compared with those of simpler models. The conformationally averaged quantum results are consistent with the empirical analysis of the Pathways model. Notably, subtle effects of quantum interference among multiple coupling pathways that arise in static structures are largely averaged out when protein thermal motion is included. Propagation through bulk water near the single-protein interface decays rapidly with distance.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein Conformation
/
Myoglobin
Type of study:
Prognostic_studies
Language:
En
Journal:
J Phys Chem B
Journal subject:
QUIMICA
Year:
2006
Document type:
Article
Affiliation country:
United States