scholarly journals Exciton Lifetime Distributions and Population Dynamics in the FMO Protein Complex from Prosthecochloris aestuarii

ACS Omega ◽  
2021 ◽  
Author(s):  
Tonu Reinot ◽  
Anton Khmelnitskiy ◽  
Adam Kell ◽  
Mahboobe Jassas ◽  
Ryszard Jankowiak
Keyword(s):  
Population Dynamics ◽  
Protein Complex ◽  
Lifetime Distributions ◽  
Prosthecochloris Aestuarii ◽  
Exciton Lifetime ◽  
Fmo Protein

On wavelength-dependent exciton lifetime distributions in reconstituted CP29 antenna of the photosystem II and its site-directed mutants

2021 ◽  
Vol 154 (8) ◽  
pp. 085101
Author(s):  
Tonu Reinot ◽  
Mahboobe Jassas ◽  
Adam Kell ◽  
Anna Paola Casazza ◽  
Stefano Santabarbara ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Lifetime Distributions ◽  
Exciton Lifetime

On the Controversial Nature of the 825 nm Exciton Band in the FMO Protein Complex

2014 ◽  
Vol 5 (8) ◽  
pp. 1450-1456 ◽  
Author(s):  
Adam Kell ◽  
Khem Acharya ◽  
Valter Zazubovich ◽  
Ryszard Jankowiak
Keyword(s):  
Protein Complex ◽  
Exciton Band ◽  
Fmo Protein ◽  
Controversial Nature

High-Resolution electron crystallography of the light-harvesting chlorophyll-a/b protein complex from chloroplast membranes

1990 ◽  
Vol 48 (1) ◽  
pp. 610-610
Author(s):  
Werner Kühlbrandt ◽  
Da Neng Wang ◽  
K.H. Downing
Keyword(s):  
High Resolution ◽  
Electron Diffraction ◽  
Chlorophyll A ◽  
Protein Complex ◽  
Structural Integrity ◽  
Light Harvesting ◽  
Lhc Ii ◽  
Diffraction Patterns ◽  
Difference Fourier ◽  
2D Crystals

The light-harvesting chlorophyll-a/b protein complex (LHC-II) is the most abundant membrane protein in the chloroplasts of green plants where it functions as a molecular antenna of solar energy for photosynthesis. We have grown two-dimensional (2d) crystals of the purified, detergent-solubilized LHC-II . The crystals which measured 5 to 10 μm in diameter were stabilized for electron microscopy by washing with a 0.5% solution of tannin. Electron diffraction patterns of untilted 2d crystals cooled to 130 K showed sharp spots to 3.1 Å resolution. Spot-scan images of 2d crystals were recorded at 160 K with the Berkeley microscope . Images of untilted crystals were processed, using the unbending procedure by Henderson et al . A projection map of the complex at 3.7Å resolution was generated from electron diffraction amplitudes and high-resolution phases obtained by image processing .A difference Fourier analysis with the same image phases and electron diffraction amplitudes recorded of frozen, hydrated specimens showed no significant differences in the 3.7Å projection map. Our tannin treatment therefore does not affect the structural integrity of the complex.

Use of Antibody to aid Visualization of Protein at the Termini of Bacteriophage Ø29 DNA

1980 ◽  
Vol 38 ◽  
pp. 540-541
Author(s):  
Dwight Anderson ◽  
Charlene Peterson ◽  
Gursaran Notani ◽  
Bernard Reilly
Keyword(s):  
Electron Microscopy ◽  
Bacillus Subtilis ◽  
Dna Synthesis ◽  
Restriction Endonuclease ◽  
Protein Complex ◽  
Protein Product ◽  
Viral Dna ◽  
Small Proteins ◽  
Antibody Labeling ◽  
Subtilis Bacteriophage

The protein product of cistron 3 of Bacillus subtilis bacteriophage Ø29 is essential for viral DNA synthesis and is covalently bound to the 5’-termini of the Ø29 DNA. When the DNA-protein complex is cleaved with a restriction endonuclease, the protein is bound to the two terminal fragments. The 28,000 dalton protein can be visualized by electron microscopy as a small dot and often is seen only when two ends are in apposition as in multimers or in glutaraldehyde-fixed aggregates. We sought to improve the visibility of these small proteins by use of antibody labeling.

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