scholarly journals Engineering a light-driven cyanine based double molecular rotor to enhance the sensitivity towards the viscous medium.

2021 ◽  
Author(s):  
Vishal Kachawal ◽  
Abhilasha Srivastava ◽  
Sumukh Thakar ◽  
Maria Zubiria-Ulacia ◽  
Diplesh Gautam ◽  
...  

This article describes the enhanced sensitivity to the viscous medium by a molecular rotor based fluorophore (RBF), TPSI I. The TPSI I molecule is designed in such a way that...

2021 ◽  
Author(s):  
Nabodita Sinha ◽  
Avinash Y. Gahane ◽  
Talat Zahra ◽  
Ashwani K. Thakur

AbstractSeed storage proteins, well-known for their nutritional functions are sequestered in protein bodies. However, their biophysical properties at the molecular level remain elusive. Based on the structure and function of protein bodies found in other organisms, we hypothesize that the seed protein bodies might be present as amyloid structures. When visualized with a molecular rotor Thioflavin-T and a recently discovered Proteostat® probe with enhanced sensitivity, the seed sections showed amyloid-like signatures in the protein storage bodies of the aleurone cells of monocots and cotyledon cells of dicots. To make the study compliant for amyloid detection, gold-standard Congo red dye was used. Positive apple-green birefringence due to Congo red affinity in some of the areas of ThT and Proteostat® binding, suggests the presence of both amyloid-like and amyloid deposits in the protein storage bodies. Further, diminishing amyloid signature in germinating seeds implies the degradation of these amyloid structures and their utilization. This study will open new research avenues for a detailed molecular-level understanding of the formation and utilization of aggregated protein bodies as well as their evolutionary roles.


2003 ◽  
Author(s):  
Cynthia L. Pickett ◽  
Wendi L. Gardner ◽  
Megan Knowles

Analgesia ◽  
1995 ◽  
Vol 1 (4) ◽  
pp. 461-464 ◽  
Author(s):  
A. Honkanen ◽  
E.R. Korpi ◽  
L. Ahtee
Keyword(s):  

2019 ◽  
Vol 16 (4) ◽  
pp. 267-276
Author(s):  
Qurat ul Ain Farooq ◽  
Noor ul Haq ◽  
Abdul Aziz ◽  
Sara Aimen ◽  
Muhammad Inam ul Haq

Background: Mass spectrometry is a tool used in analytical chemistry to identify components in a chemical compound and it is of tremendous importance in the field of biology for high throughput analysis of biomolecules, among which protein is of great interest. Objective: Advancement in proteomics based on mass spectrometry has led the way to quantify multiple protein complexes, and proteins interactions with DNA/RNA or other chemical compounds which is a breakthrough in the field of bioinformatics. Methods: Many new technologies have been introduced in electrospray ionization (ESI) and Matrixassisted Laser Desorption/Ionization (MALDI) techniques which have enhanced sensitivity, resolution and many other key features for the characterization of proteins. Results: The advent of ambient mass spectrometry and its different versions like Desorption Electrospray Ionization (DESI), DART and ELDI has brought a huge revolution in proteomics research. Different imaging techniques are also introduced in MS to map proteins and other significant biomolecules. These drastic developments have paved the way to analyze large proteins of >200kDa easily. Conclusion: Here, we discuss the recent advancement in mass spectrometry, which is of great importance and it could lead us to further deep analysis of the molecules from different perspectives and further advancement in these techniques will enable us to find better ways for prediction of molecules and their behavioral properties.


BioTechniques ◽  
2004 ◽  
Vol 36 (2) ◽  
pp. 334-336 ◽  
Author(s):  
Keqin Gregg ◽  
Wenli Zhou ◽  
Wan Ji ◽  
Sara Davis
Keyword(s):  

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Arkadiusz Miazek ◽  
Michał Zalas ◽  
Joanna Skrzymowska ◽  
Bryan A. Bogin ◽  
Krzysztof Grzymajło ◽  
...  

AbstractThe neuronal membrane-associated periodic spectrin skeleton (MPS) contributes to neuronal development, remodeling, and organization. Post-translational modifications impinge on spectrin, the major component of the MPS, but their role remains poorly understood. One modification targeting spectrin is cleavage by calpains, a family of calcium-activated proteases. Spectrin cleavage is regulated by activated calpain, but also by the calcium-dependent binding of calmodulin (CaM) to spectrin. The physiologic significance of this balance between calpain activation and substrate-level regulation of spectrin cleavage is unknown. We report a strain of C57BL/6J mice harboring a single αII spectrin point mutation (Sptan1 c.3293G > A:p.R1098Q) with reduced CaM affinity and intrinsically enhanced sensitivity to calpain proteolysis. Homozygotes are embryonic lethal. Newborn heterozygotes of either gender appear normal, but soon develop a progressive ataxia characterized biochemically by accelerated calpain-mediated spectrin cleavage and morphologically by disruption of axonal and dendritic integrity and global neurodegeneration. Molecular modeling predicts unconstrained exposure of the mutant spectrin’s calpain-cleavage site. These results reveal the critical importance of substrate-level regulation of spectrin cleavage for the maintenance of neuronal integrity. Given that excessive activation of calpain proteases is a common feature of neurodegenerative disease and traumatic encephalopathy, we propose that damage to the spectrin MPS may contribute to the neuropathology of many disorders.


2021 ◽  
Author(s):  
Meng Yang ◽  
Feng Xie ◽  
Shan-Shan Li ◽  
Chu-Hong Lin ◽  
Xing-Jiu Huang ◽  
...  

A novel zero-valent iron nanomaterial (Fe0@Fe2MnO4) was synthesized and achieved an ultrasensitive electrochemical detection of As(III). It was found that the enhanced sensitivity is attributed to the surficial catalytic redox...


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