Results 11 to 20 of about 3,652,274 (296)

Native protein denaturation using urea

open access: yesBioTechniques, 2017
Protocol Summary Here we present a new protocol to analyze protein unfolding kinetics using a quantified real-time thermocycler. This technique enables the analysis of a wide range of denaturants (and their interactions with temperature change) on ...
Kyle K. Biggar   +2 more
doaj   +2 more sources

Measurement of Heat and Pressure Induced Denaturation of Whey Protein Isolate Using Reversed-Phase HPLC and FTIR-Spectroscopy [PDF]

open access: yesTrends in Peptide and Protein Sciences, 2019
The protein molecules experience various external stresses leading to denaturation of protein during the process of transforming original whey to the concentrated whey proteins or while the concentrated proteins are used in the protein-enriched food ...
Md. Amdadul Haque   +3 more
doaj   +2 more sources

Studying Protein-Ligand Interactions by Protein Denaturation and Quantitative Cross-Linking Mass Spectrometry. [PDF]

open access: yesAnal Chem, 2023
Recently, several mass spectrometry methods have utilized protein structural stability for the quantitative study of protein–ligand engagement. These protein-denaturation approaches, which include thermal proteome profiling (TPP) and stability of ...
Mathay M, Keller A, Bruce JE.
europepmc   +2 more sources

Recipes for inducing cold denaturation in an otherwise stable protein. [PDF]

open access: yes, 2022
Although cold denaturation is a fundamental phenomenon common to all proteins, it can only be observed in a handful of cases where it occurs at temperatures above the freezing point of water.
Giorgio Colombo (65952)   +6 more
core   +4 more sources

Protein Denaturation Zero Entropy Temperature, and the Structure of Water Around Hydrophobic and Amphiphilic Solutes [PDF]

open access: yes, 2020
The hydrophobic effect plays a key role in many chemical and biological processes, including protein folding. Nonetheless, a comprehensive picture of the effect of temperature on hydrophobic hydration and protein denaturation remains elusive.
Nuno, Galamba, kazimieras, Tamoliūnas
core   +1 more source

The molecular basis of the effect of temperature on enzyme activity [PDF]

open access: yes, 2010
Experimental data show that the effect of temperature on enzymes cannot be adequately explained in terms of a two-state model based on increases in activity and denaturation.
Oudshoorn, Matthew Leslie   +17 more
core   +1 more source

POTENSI ANTIINFLAMASI JUS BUAH BELIMBING (Averrhoa carambola L.) TERHADAP DENATURASI PROTEIN IN VITRO

open access: yesBerkala Kedokteran, 2015
Starfruit (Averrhoa carambola L.) is an Asian tree that has been used in traditional medicine. Flavonoids, saponins, and tannins is thought to have antiinflammatory in inhibiting protein denaturation.
Farizka Erianti   +2 more
doaj   +1 more source

Differential denaturation of serum proteome reveals a significant amount of hidden information in complex mixtures of proteins. [PDF]

open access: yesPLoS ONE, 2013
UNLABELLED: Recently developed proteomic technologies allow to profile thousands of proteins within a high-throughput approach towards biomarker discovery, although results are not as satisfactory as expected.
Vincenzo Verdoliva   +10 more
doaj   +1 more source

Non-Thermal Processing of a Protein Functional Beverage Using Pulsed Electric Fields: Escherichia coli Inactivation and Effect on Proteins

open access: yesBeverages, 2022
The application of pulsed electric fields (PEFs) for the inactivation of Escherichia coli, suspended in a protein shake beverage and diluted with sterilized distilled water was carried out. Square bipolar pulses in the range of 25–40 kV/cm electric field
Mona Alzahrani   +2 more
doaj   +1 more source

Single-molecule chemical denaturation of riboswitches [PDF]

open access: yes, 2013
To date, single-molecule RNA science has been developed almost exclusively around the effect of metal ions as folding promoters and stabilizers of the RNA structure.
St-Pierre, Patrick   +14 more
core   +1 more source

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