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.

Book Review

2014 ◽  
Vol 11 (3) ◽  
pp. 387-390
Author(s):  
Antonina Levatino
Keyword(s):  
Control Strategies ◽  
Human Mobility ◽  
Diverse Range ◽  
Transnational Mobility ◽  
Migration Management ◽  
Nation States ◽  
Migration Control ◽  
Political Economic ◽  
Controversial Nature

Martin Geiger & Antoine Pécoud (eds.), Disciplining the Transnational Mobility of People, Palgrave Macmillan, 2013, 271 pp., (ISBN 978-1-137-26306-3).In the last decades a very diverse range of initiatives have been undertaken in order to intensify and diversify the ways human mobility is managed and restricted. This trend towards a ‘diversification’ of the migration control strategies stems from the increased awareness by the nation-states of the profoundly controversial nature of the migration management enterprise because of its political, economic, social and moral implications.

ASSOCIATION BEHAVIOUR OF THE OESTRADIOL-BINDING PROTEIN COMPLEX WITH THE NUCLEAR FRACTION

1972 ◽  
Vol 71 (2_Suppla) ◽  
pp. S420-S438 ◽  
Author(s):  
David L. Williams ◽  
Jack Gorski
Keyword(s):  
Binding Site ◽  
Protein Complex ◽  
Binding Protein ◽  
Nuclear Fraction ◽  
Site Saturation ◽  
Total Binding

ABSTRACT A number of studies have been carried out to examine the distribution of the oestradiol-binding protein complex between cytosol and nuclear fractions as a function of total binding site saturation. The results of these studies suggest that each binding protein has one binding site for the hormone. In addition, these studies suggest that the interaction of the oestradiol-binding protein complex with the nucleus involves a large number of low affinity association sites.

Protein Flexibility Catalyzes a Cell Signaling Reaction of the Ras-GAP Complex

2019 ◽  
Author(s):  
Keiei Kumon ◽  
Masahiro Higashi ◽  
Shinji Saito ◽  
Shigehiko Hayashi
Keyword(s):  
Cell Signaling ◽  
Conformational Changes ◽  
Catalytic Reaction ◽  
Protein Complex ◽  
Enzyme Mechanism ◽  
Activation Free Energy ◽  
Chemical Catalysis ◽  
Simple Chemical ◽  
A Cell ◽  
Enzyme Molecules

Many enzyme molecules exhibit characteristic global and slow dynamics which furnish them with allostery realizing remarkable molecular functionalities more than simple chemical catalysis. However, molecular mechanism of a catalytic reaction associated with the molecular flexibility of enzymes is not well-understood. Here we report a hybrid molecular simulation study on GTPase activity of a Ras-GAP protein complex for cell signaling termination. We unveiled that extensive conformational changes of the protein complex and exclusion of internal water molecules are induced upon the transition state (TS) formation in the catalytic reaction and significantly lower the reaction activation free energy. We also revealed that tumor-related mutations perturb those conformational changes upon the TS formation, leading to reduction of the catalytic activity. The findings of the remarkably dynamic protein conformation directly linking to the catalytic reaction have broad implications for understanding of enzyme mechanism and for developments of allosteric drugs and novel catalysts.

‘... Call the Mute Artifacts to Speech’: New Essays on the History of Archeology

2018 ◽  
pp. 1274-1279
Author(s):  
Elena V. Olimpieva ◽  
Keyword(s):  
20Th Century ◽  
Comparative Method ◽  
Early 20Th Century ◽  
Historical Overview ◽  
Historical Experience ◽  
Historical Material ◽  
Manuscript Tradition ◽  
History Of ◽  
Publication Practices ◽  
Controversial Nature

The article reviews O. A. Shashkova’s ‘... Call the Mute Artifacts to Speech.’ Essays on the History of Archaeography of the 15th - Early 20th Century. Wide array of sources and broad geographical frameworks allow Shashkova to present emergence and development of Russian and European archaeography from the 15th to early 20th century intelligibly enough for educational purposes. A whole chapter is devoted to the manuscript tradition and publishing of sources before Gutenberg. When considering the formation of archaeographical tradition, the author uses comparative method. O. A. Shashkova offers a historical overview and analyzes theoretical and practical issues of archaeography. The reviewer notes the significance of the chosen topic due to a need to reconsider the development of publishing in light of modern views on archaeography and to make it accessible to students and non-professionals. She notes traditional academic approach of O. A. Shashkova to presentation of the development publication practices. The review considers the possibility of using the ‘Essays...’ in studying the history of archaeography and offers possible directions for a broader consideration of historical experience, in particular, of Novikov’s publication projects. The review notes the controversial nature of the author’s approach to systematization of her large historical material in order to consider issues concerning the study of archaeographical practices. It stresses that coverage of issues of development of methods of preparation of publications separately from its historical and practical aspects hinders successful mastering of the material by an untrained reader. It concludes that the publication has high practical value for specialists in archaeography and students.

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