Document Detail


Impact of assembly state on the defect tolerance of TMV-based light harvesting arrays.
MedLine Citation:
PMID:  20392093     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Self-assembling, light harvesting arrays of organic chromophores can be templated using the tobacco mosaic virus coat protein (TMVP). The efficiency of energy transfer within systems containing a high ratio of donors to acceptors shows a strong dependence on the TMVP assembly state. Rod and disk assemblies derived from a single stock of chromophore-labeled protein exhibit drastically different levels of energy transfer, with rods significantly outperforming disks. The origin of the superior transfer efficiency was probed through the controlled introduction of photoinactive conjugates into the assemblies. The efficiency of the rods showed a linear dependence on the proportion of deactivated chromophores, suggesting the availability of redundant energy transfer pathways that can circumvent defect sites. Similar disk-based systems were markedly less efficient at all defect levels. To examine these differences further, the brightness of donor-only systems was measured as a function of defect incorporation. In rod assemblies, the photophysical properties of the donor chromophores showed a significant dependence on the number of defects. These differences can be partly attributed to vertical energy transfer events in rods that occur more rapidly than the horizontal transfers in disks. Using these geometries and the previously measured energy transfer rates, computational models were developed to understand this behavior in more detail and to guide the optimization of future systems. These simulations have revealed that significant differences in excited state dissipation rates likely also contribute to the greater efficiency of the rods and that statistical variations in the assembly process play a more minor role.
Authors:
Rebekah A Miller; Nicholas Stephanopoulos; Jesse M McFarland; Andrew S Rosko; Phillip L Geissler; Matthew B Francis
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  132     ISSN:  1520-5126     ISO Abbreviation:  J. Am. Chem. Soc.     Publication Date:  2010 May 
Date Detail:
Created Date:  2010-04-28     Completed Date:  2010-07-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6068-74     Citation Subset:  IM    
Affiliation:
Department of Chemistry, University of California, Berkeley, and Materials Sciences Division, Lawrence Berkeley National Laboratories, Berkeley, California 94720-1460, USA.
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MeSH Terms
Descriptor/Qualifier:
Capsid Proteins / chemistry*
Energy Transfer
Light
Light-Harvesting Protein Complexes / chemistry*
Photobleaching
Protein Array Analysis
Tobacco Mosaic Virus / chemistry*
Grant Support
ID/Acronym/Agency:
1T32GMO66698//PHS HHS
Chemical
Reg. No./Substance:
0/Capsid Proteins; 0/H protein, Tobacco mosaic virus; 0/Light-Harvesting Protein Complexes

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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