Imaging Switchable Protein Interactions With an Active Porous Polymer Support

2020 ◽  
Author(s):  
Chayan Dutta ◽  
Logan D. C. Bishop ◽  
Jorge Zepeda O ◽  
Sudeshna Chatterjee ◽  
Charlotte Flatebo ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Porous Polymer ◽  
Polymer Support

Imaging Switchable Protein Interactions with an Active Porous Polymer Support

2020 ◽  
Vol 124 (22) ◽  
pp. 4412-4420 ◽  
Author(s):  
Chayan Dutta ◽  
Logan D. C. Bishop ◽  
Jorge Zepeda O ◽  
Sudeshna Chatterjee ◽  
Charlotte Flatebo ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Porous Polymer ◽  
Polymer Support

scholarly journals Correction to “Imaging Switchable Protein Interactions with an Active Porous Polymer Support”

2021 ◽  
Author(s):  
Chayan Dutta ◽  
Logan D. C. Bishop ◽  
Jorge Zepeda O ◽  
Sudeshna Chatterjee ◽  
Charlotte Flatebo ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Porous Polymer ◽  
Polymer Support

Silver nanoparticles stabilized in porous polymer support: A highly active catalytic nanoreactor

2016 ◽  
Vol 524 ◽  
pp. 214-222 ◽  
Author(s):  
Sabyasachi Patra ◽  
Apurva N. Naik ◽  
Ashok K. Pandey ◽  
Debasis Sen ◽  
S. Mazumder ◽  
...  
Keyword(s):  
Silver Nanoparticles ◽  
Porous Polymer ◽  
Polymer Support ◽  
Highly Active

scholarly journals Design of a Semi-Continuous Selective Layer Based on Deposition of UiO-66 Nanoparticles for Nanofiltration

Membranes ◽  
2018 ◽  
Vol 8 (4) ◽  
pp. 129 ◽  
Author(s):  
Goji Shangkum ◽  
Patchanee Chammingkwan ◽  
Dai Trinh ◽  
Toshiaki Taniike
Keyword(s):  
External Surface ◽  
Metal Organic Framework ◽  
Composite Membranes ◽  
Porous Polymer ◽  
Water Filtration ◽  
Polymer Support ◽  
Particle Sizes ◽  
External Surface Area ◽  
Selective Layer ◽  
Metal Organic

Deposition of UiO-66 metal–organic framework nanoparticles onto a porous polymer support is a promising approach to designing highly-permeable, size-selective, flexible, and stable membranes for water filtration. In this article, a series of UiO-66 nanoparticles having different particle sizes were synthesized and employed to prepare UiO-66-deposited composite membranes. It was found that the size of the UiO-66 nanoparticles had great influences on the performance of the composite membranes for the filtration of a methylene blue aqueous solution. The deposition of smaller nanoparticles afforded a selective layer having a greater external surface area and narrower interparticle voids. These features made the deposition of smaller nanoparticles more advantageous in terms of the flux and rejection, while the deposition of greater nanoparticles afforded a selective layer more tolerant for fouling. Bimodal composite membranes were prepared by depositing mixed UiO-66 nanoparticles of smaller and bigger sizes. These membranes successfully combined the advantages of nanoparticles of a distinct size.

Characterization of microtubules by dark-field STEM and replication

1991 ◽  
Vol 49 ◽  
pp. 152-153
Author(s):  
S.B. Andrews ◽  
R.D. Leapman ◽  
P.E. Gallant ◽  
T.S. Reese
Keyword(s):  
Protein Interactions ◽  
Low Dose ◽  
Unit Length ◽  
Dark Field ◽  
Carbon Films ◽  
Microtubule Associated Proteins ◽  
Molecular Weights ◽  
Freeze Dried ◽  
Protein Motors ◽  
Associated Proteins

As part of a study on protein interactions involved in microtubule (MT)-based transport, we used the VG HB501 field-emission STEM to obtain low-dose dark-field mass maps of isolated, taxol-stabilized MTs and correlated these micrographs with detailed stereo images from replicas of the same MTs. This approach promises to be useful for determining how protein motors interact with MTs. MTs prepared from bovine and squid brain tubulin were purified and free from microtubule-associated proteins (MAPs). These MTs (0.1-1 mg/ml tubulin) were adsorbed to 3-nm evaporated carbon films supported over Formvar nets on 600-m copper grids. Following adsorption, the grids were washed twice in buffer and then in either distilled water or in isotonic or hypotonic ammonium acetate, blotted, and plunge-frozen in ethane/propane cryogen (ca. -185 C). After cryotransfer into the STEM, specimens were freeze-dried and recooled to ca.-160 C for low-dose (<3000 e/nm2) dark-field mapping. The molecular weights per unit length of MT were determined relative to tobacco mosaic virus standards from elastic scattering intensities. Parallel grids were freeze-dried and rotary shadowed with Pt/C at 14°.

Role of small nuclear RNAs in eukaryotic gene expression

2013 ◽  
Vol 54 ◽  
pp. 79-90 ◽  
Author(s):  
Saba Valadkhan ◽  
Lalith S. Gunawardane
Keyword(s):  
Gene Expression ◽  
Protein Interactions ◽  
Rna Stability ◽  
Splice Sites ◽  
Branch Site ◽  
Small Nuclear Rnas ◽  
Eukaryotic Gene Expression ◽  
Eukaryotic Gene ◽  
Rna Biogenesis

Eukaryotic cells contain small, highly abundant, nuclear-localized non-coding RNAs [snRNAs (small nuclear RNAs)] which play important roles in splicing of introns from primary genomic transcripts. Through a combination of RNA–RNA and RNA–protein interactions, two of the snRNPs, U1 and U2, recognize the splice sites and the branch site of introns. A complex remodelling of RNA–RNA and protein-based interactions follows, resulting in the assembly of catalytically competent spliceosomes, in which the snRNAs and their bound proteins play central roles. This process involves formation of extensive base-pairing interactions between U2 and U6, U6 and the 5′ splice site, and U5 and the exonic sequences immediately adjacent to the 5′ and 3′ splice sites. Thus RNA–RNA interactions involving U2, U5 and U6 help position the reacting groups of the first and second steps of splicing. In addition, U6 is also thought to participate in formation of the spliceosomal active site. Furthermore, emerging evidence suggests additional roles for snRNAs in regulation of various aspects of RNA biogenesis, from transcription to polyadenylation and RNA stability. These snRNP-mediated regulatory roles probably serve to ensure the co-ordination of the different processes involved in biogenesis of RNAs and point to the central importance of snRNAs in eukaryotic gene expression.

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