Size dependent correlation between structure and apparent stiffness of viral DNA during temperature variation

2021 ◽  
pp. 104501
Author(s):  
Cheng-Yin Zhang ◽  
Neng-Hui Zhang
Keyword(s):  
Temperature Variation ◽  
Viral Dna ◽  
Size Dependent ◽  
Apparent Stiffness ◽  
Dependent Correlation

scholarly journals Actin crosslinker competition and sorting drive emergent GUV size-dependent actin network architecture

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Yashar Bashirzadeh ◽  
Steven A. Redford ◽  
Chatipat Lorpaiboon ◽  
Alessandro Groaz ◽  
Hossein Moghimianavval ◽  
...  
Keyword(s):  
Network Architecture ◽  
Molecular Size ◽  
Coarse Grained ◽  
General Mechanism ◽  
Complex Structures ◽  
Actin Bundles ◽  
Size Dependent ◽  
Apparent Stiffness ◽  
Coarse Grained Simulations

AbstractThe proteins that make up the actin cytoskeleton can self-assemble into a variety of structures. In vitro experiments and coarse-grained simulations have shown that the actin crosslinking proteins α-actinin and fascin segregate into distinct domains in single actin bundles with a molecular size-dependent competition-based mechanism. Here, by encapsulating actin, α-actinin, and fascin in giant unilamellar vesicles (GUVs), we show that physical confinement can cause these proteins to form much more complex structures, including rings and asters at GUV peripheries and centers; the prevalence of different structures depends on GUV size. Strikingly, we found that α-actinin and fascin self-sort into separate domains in the aster structures with actin bundles whose apparent stiffness depends on the ratio of the relative concentrations of α-actinin and fascin. The observed boundary-imposed effect on protein sorting may be a general mechanism for creating emergent structures in biopolymer networks with multiple crosslinkers.

Size-Dependent Temperature Variation of the Energy Gap in Lead-Salt Quantum Dots

1998 ◽  
Vol 81 (16) ◽  
pp. 3539-3542 ◽  
Author(s):  
A. Olkhovets ◽  
R.-C. Hsu ◽  
A. Lipovskii ◽  
F. W. Wise
Keyword(s):  
Quantum Dots ◽  
Temperature Variation ◽  
Energy Gap ◽  
Lead Salt ◽  
Size Dependent

Production and STEM examination of controlled-size silver clusters

1983 ◽  
Vol 41 ◽  
pp. 338-339
Author(s):  
M. A. Listvan ◽  
R. P. Andres
Keyword(s):  
Cluster Size ◽  
Metal Clusters ◽  
Experimental Parameter ◽  
Carbon Films ◽  
Metal Species ◽  
Silver Clusters ◽  
Free Jet ◽  
Size Dependent ◽  
Cluster Properties ◽  
Controllable Size

Knowledge of the function and structure of small metal clusters is one goal of research in catalysis. One important experimental parameter is cluster size. Ideally, one would like to produce metal clusters of regulated size in order to characterize size-dependent cluster properties.A source has been developed which is capable of producing microscopic metal clusters of controllable size (in the range 5-500 atoms) This source, the Multiple Expansion Cluster Source, with a Free Jet Deceleration Filter (MECS/FJDF) operates as follows. The bulk metal is heated in an oven to give controlled concentrations of monomer and dimer which were expanded sonically. These metal species were quenched and condensed in He and filtered to produce areosol particles of a controlled size as verified by mass spectrometer measurements. The clusters were caught on pre-mounted, clean carbon films. The grids were then transferred in air for microscopic examination. MECS/FJDF was used to produce two different sizes of silver clusters for this study: nominally Ag6 and Ag50.

Transfer Technique for Electron Microscopy of Membrance Filter Samples

1974 ◽  
Vol 32 ◽  
pp. 554-555
Author(s):  
Lawrence W. Ortiz ◽  
Bonnie L. Isom
Keyword(s):  
Electron Microscopy ◽  
Electron Microscope ◽  
Pore Size ◽  
Membrane Filters ◽  
Size Dependent

A procedure is described for the quantitative transfer of fibers and particulates collected on membrane filters to electron microscope (EM) grids. Various Millipore MF filters (Millipore AA, HA, GS, and VM; 0.8, 0.45, 0.22 and 0.05 μm mean pore size) have been used with success. Observed particle losses have not been size dependent and have not exceeded 10%. With fibers (glass or asbestos) as the collected media this observed loss is approximately 3%.

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.

The infection and viral DNA replication ofBocavirusminute virus of canine in permissive cells and non-permissive cells

2010 ◽  
Vol 34 (8) ◽  
pp. S60-S60
Author(s):  
Yuning Sun ◽  
Fang Li ◽  
Jianming Qiu ◽  
Xiaohong Lu
Keyword(s):  
Dna Replication ◽  
Viral Dna ◽  
Viral Dna Replication

Spindle scaling mechanisms

2020 ◽  
Vol 64 (2) ◽  
pp. 383-396
Author(s):  
Lara K. Krüger ◽  
Phong T. Tran
Keyword(s):  
Cell Size ◽  
Spindle Assembly ◽  
Dependent Manner ◽  
Post Translational Modification ◽  
Size Dependent ◽  
A Cell ◽  
Chromosome Separation ◽  
Spindle Elongation ◽  
Protein Gradients ◽  
Spindle Structure

Abstract The mitotic spindle robustly scales with cell size in a plethora of different organisms. During development and throughout evolution, the spindle adjusts to cell size in metazoans and yeast in order to ensure faithful chromosome separation. Spindle adjustment to cell size occurs by the scaling of spindle length, spindle shape and the velocity of spindle assembly and elongation. Different mechanisms, depending on spindle structure and organism, account for these scaling relationships. The limited availability of critical spindle components, protein gradients, sequestration of spindle components, or post-translational modification and differential expression levels have been implicated in the regulation of spindle length and the spindle assembly/elongation velocity in a cell size-dependent manner. In this review, we will discuss the phenomenon and mechanisms of spindle length, spindle shape and spindle elongation velocity scaling with cell size.

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