Results 31 to 40 of about 3,652,274 (296)

The Effects of Storage on Quality and Nutritional Values of Ehrenberg’s Snapper Muscles (Lutjanus Ehrenbergi): Evaluation of Natural Antioxidants Effect on the Denaturation of Proteins

open access: yesBiomolecules, 2019
: Protein denaturation in frozen minced fillets (Ehrenberg’s Snapper), stored at −25°C was studied; 50.0 mg biomass/50g mince fillets treated with cinnamon, cumin, turmeric, garlic, ginger and 25.0 mg of vitamin C were used to slow ...
Abdelaziz Elgamouz   +5 more
doaj   +1 more source

Chemical shifts in denatured proteins: Resonance assignments for denatured ubiquitin and comparisons with other denatured proteins

open access: yesJournal of Biomolecular NMR, 2001
Chemical shift assignment is reported for the protein ubiquitin denatured in 8M urea at pH 2. The variations in 15N chemical shifts of three different proteins (ubiquitin, disulfide reduced, carboxymethylated lysozyme, all-Ala-alpha-lactalbumin), all without disulfides and denatured in 8M urea at pH 2 are compared to 'random coil shifts' of small model
Peti, W   +3 more
openaire   +3 more sources

Use of Microwave Radiometry to Monitor Thermal Denaturation of Albumin

open access: yesFrontiers in Physiology, 2018
This study monitored thermal denaturation of albumin using microwave radiometry. Brightness Temperature, derived from Microwave Emission (BTME) of an aqueous solution of bovine serum albumin (0.1 mM) was monitored in the microwave frequency range 3.8–4.2
Yuri Ivanov   +11 more
doaj   +1 more source

New Natural Injection-Moldable Composite Material from Sunflower Oil Cake [PDF]

open access: yes, 2006
Through a twin-screw extrusion process the native structure of sunflower oil cake was completely transformed (globular protein denaturation/texturization and husk fiber defibration) into a simpler matrix-fiber structure, as could be seen on SEM ...
O. Orliac   +7 more
core   +1 more source

Salting the charged surface: pH and salt dependence of protein G B1 stability. [PDF]

open access: yes, 2006
This study shows significant effects of protein surface charges on stability and these effects are not eliminated by salt screening. The stability for a variant of protein G B1 domain was studied in the pH-range of 1.5-11 at low, 0.15 M, and 2 M salt ...
Xue, Wei-Feng   +19 more
core   +1 more source

Isothermal chemical denaturation as a complementary tool to overcome limitations of thermal differential scanning fluorimetry in predicting physical stability of protein formulations [PDF]

open access: yes, 2018
Various stability indicating techniques find application in the early stage development of novel therapeutic protein candidates. Some of these techniques are used to select formulation conditions that provide high protein physical stability.
Winter, Gerhard   +5 more
core   +1 more source

ANTI-INFLAMMATORY ACTIVITY OF ETHANOL EXTRACT AND ETHYL ACETATE FRACTION OF KEBIUL (Caesalpinia bonduc L.) SEED COAT AGAINST INHIBITION OF PROTEIN DENATURATION

open access: yesJurnal Kimia Riset, 2022
Inflammation is a normal protective reaction against tissue damage caused by physical injury, harmful chemicals, and protein denaturation. Protein denaturation is a process in which proteins lose their tertiary structure and secondary structure due to ...
Dwi Fitriyani, Raden Fatahillah
doaj   +1 more source

Immunological Characteristics of Denatured Proteins [PDF]

open access: yesNature, 1966
AFTER denaturation, some characteristic changes occur in the properties of proteins, among which are variations in immunological features. For example, the specific immunological behaviour of ovalbumin is altered and its antigenic capacity decreases considerably1–3.
openaire   +3 more sources

Determination of Pseudokinase-ligand Interaction by a Fluorescence-based Thermal Shift Assay

open access: yesBio-Protocol, 2014
This protocol describes a robust technique for the measurement of pseudokinase-ligand interaction by a fluorescence-based Thermal Shift Assay (TSA).
Isabelle Lucet   +7 more
doaj   +1 more source

Polar or apolar--the role of polarity for urea-induced protein denaturation. [PDF]

open access: yesPLoS Computational Biology, 2008
Urea-induced protein denaturation is widely used to study protein folding and stability; however, the molecular mechanism and driving forces of this process are not yet fully understood.
Martin C Stumpe, Helmut Grubmüller
doaj   +1 more source

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