Cold Denaturation of Proteins: Where Bioinformatics Meets Thermodynamics to Offer a Mechanistic Understanding: Pea Protein As a Case Study

2021 ◽  
Author(s):  
Harrison Helmick ◽  
Hazal Turasan ◽  
Merve Yildirim ◽  
Arun Bhunia ◽  
Andrea Liceaga ◽  
...  
Keyword(s):  
Pea Protein ◽  
Cold Denaturation ◽  
Mechanistic Understanding ◽  
Denaturation Of Proteins

Mechanistic understanding of the sensing process by analyzing response curves of TiO2 based humidity sensors

2021 ◽  
Vol 12 (4) ◽  
pp. 045010
Author(s):  
Balaji Rakesh ◽  
Nipun Sharma ◽  
Rupali Nagar ◽  
Vipul Dhongade ◽  
Krishna Daware ◽  
...  
Keyword(s):  
Food Packaging ◽  
Sol Gel ◽  
Fast Response ◽  
Response Curves ◽  
Initial State ◽  
Sensing Material ◽  
Adsorption Processes ◽  
Low Humidity ◽  
Mechanistic Understanding

Abstract Sensors function by interacting with an appropriate stimulus, undergo a change in property, which is then diagnosed by making some measurements. For any sensor, the type of interaction between analyte and sensor surface determines its overall performance. This article explores the philosophy in which primary measurements like response curves can hold information on the “type” of interaction occurring between analyte and sensing material. As case study, titanium oxide (TiO2) pellet sensors fabricated by sol-gel growth of TiO2 nanoparticles (as-grown and annealed) are investigated for humidity sensing at room temperature. The sensors display a very fast response in the 0%–30% relative humidity (%RH) range and return to their initial state without applying any external heat treatment. The response curves are analysed in view of adsorption processes guided by Langmuir isotherms. Correlation between sensor microstructure, adsorption processes and response curve is used to build the mechanistic understanding of the sensing process. The results bring out a unique correlation between sensor microstructure, interaction of analyte with sensing material and profile of response curves. Further, the synthesised sensors exhibit a linear response in the 0%–30% RH range making them suitable for low humidity environments like food packaging industry.

Heightened Cold-Denaturation of Proteins at the Ice–Water Interface

2020 ◽  
Vol 142 (12) ◽  
pp. 5722-5730 ◽  
Author(s):  
Andrea Arsiccio ◽  
James McCarty ◽  
Roberto Pisano ◽  
Joan-Emma Shea
Keyword(s):  
Water Interface ◽  
Cold Denaturation ◽  
Ice Water ◽  
Denaturation Of Proteins

scholarly journals The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin

2019 ◽  
Vol 150 (7) ◽  
pp. 075102 ◽  
Author(s):  
Yanis R. Espinosa ◽  
Ernesto R. Caffarena ◽  
J. Raúl Grigera
Keyword(s):  
High Pressure ◽  
Cold Denaturation ◽  
Denaturation Of Proteins

scholarly journals Heat, Cold and Pressure Induced Denaturation of Proteins

2003 ◽  
Vol 17 (2-3) ◽  
pp. 367-376 ◽  
Author(s):  
G. Panick ◽  
H. Herberhold ◽  
Z. Sun ◽  
R. Winter
Keyword(s):  
Infrared Spectroscopy ◽  
Secondary Structure ◽  
Structural Properties ◽  
Relaxation Technique ◽  
Cold Denaturation ◽  
Unfolded State ◽  
Fouriertransform Infrared Spectroscopy ◽  
Monomeric Proteins ◽  
Kinetics Of ◽  
Denaturation Of Proteins

We studied the pressureinduced unfolding and refolding of monomeric proteins, such as SNase, αchymotrypsin and ubiquitin, by using synchrotron Xray smallangle scattering and Fouriertransform infrared spectroscopy, which monitor changes in the tertiary and secondary structural properties of the proteins upon pressurization. Furthermore, by using the pressurejump relaxation technique in combination with timeresolved Xray diffraction and infrared spectroscopy, the kinetics of the unfolding/refolding of the proteins, was investigated. Significant differences in secondary structure and chain compactness in the folding/unfolding reactions of these proteins are observed. The results are compared with data obtained from other methods of denaturation, such as heat and pressure-assisted cold denaturation. The cold- and pressure-induced unfolding both yield a particularly unfolded state characterized by a persistent amount of secondary structure.

Hot and cold denaturation of proteins: Critical aspects

1999 ◽  
Vol 10 (1) ◽  
pp. 193-196 ◽  
Author(s):  
A. Hansen ◽  
M.H. Jensen ◽  
K. Sneppen ◽  
G. Zocchi
Keyword(s):  
Cold Denaturation ◽  
Denaturation Of Proteins ◽  
Critical Aspects
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