How does coomasssie dye reacts with proteins?
Best insight from top research papers
Coomassie Brilliant Blue dye interacts with proteins in various ways. It forms stable complexes with individual proteins, resulting in a classic protein-dye complex with an absorption maximum at 595 nm . However, in the case of glycine transporters 1 and 2 N-termini, an atypical dynamic interaction with Coomassie dye is observed. This interaction interferes with the Bradford assay, leading to a decrease in absorption at 595 nm and an increase in absorbance shoulders above 300 and 700 nm . The dynamic properties of these protein-dye complexes may be a signature of high flexibility and protein disorder . Additionally, Coomassie Brilliant Blue dye can be used for staining proteins with high sensitivity and preventing background staining . Blue native gel electrophoresis utilizes Coomassie Brilliant Blue G-250 to visualize proteins, but caution is needed when using iodoacetamide conjugated to biotin (BIAM) as it can interfere with Coomassie blue staining . A fixation-free and fast protein-staining method for gel electrophoresis using Coomassie blue is also described, which offers speed, simplicity, and low cost . The Coomassie Brilliant Blue Assay can be used for the detection and quantitative measurement of proteins, with improved sensitivity and linearity over a broad range .
Answers from top 3 papers
More filters
| Papers (3) | Insight |
|---|---|
2 Citations | The paper does not provide information on how Coomassie dye reacts with proteins. The paper discusses the interference of dimethylformamide (DMF) with Coomassie blue G staining of proteins during blue native gel electrophoresis (BN-PAGE). |
7 Citations | The paper states that Coomassie Brilliant Blue interacts with proteins, but the specific reaction mechanism is not described. |
| The paper does not provide information on how Coomassie dye reacts with proteins. |
Related Questions
What is needed for protein adsorption?4 answersProtein adsorption requires various factors such as surface functionalities, charged polymers, and specific materials. Different methods like physical adsorption, non-covalent adsorption, and chemical covalent binding effects play crucial roles in protein adsorption processes. The addition of micro/nanoparticles to a protein solution forms a protein corona, affected by pH and electrostatic interactions. Grafted charged polymers on a porous structure enhance adsorption capacity and kinetics of proteins under different conditions, influenced by polymer length, content, and salt concentration. Charge-dependent dicarboxymethyl cellulose (DCMC) successfully adsorbs positively charged proteins like cytochrome C and lysozyme, following Langmuir adsorption isotherm and pseudo second-order kinetics, with high adsorption capacities and reusability. These findings collectively highlight the importance of material properties, surface functionalities, and specific interactions in facilitating protein adsorption processes.
How catalysts react with protein?4 answersCatalysts interact with proteins in various ways. Proteins can serve as templates for the synthesis and support of metallic nanoparticles, where protein assemblies facilitate the reduction of metal salts to obtain nanometer-sized noble metal particles with catalytic activity in hydrogenation reactions. Additionally, enzymes can be computationally designed to promote nonbiological reactions, such as Diels-Alder cycloaddition and metal-dependent hydrolysis, providing insights into enzyme function and serving as starting points for laboratory evolution. Immobilized protein catalysts can be prepared by binding a protein layer to a polymeric support using an adhesive and a crosslinking agent, creating a stable protein catalyst system. Furthermore, a rhodium complex immobilized within a protein cage can catalyze specific reactions like the polymerization of phenylacetylene, showcasing the versatility of protein-catalyst systems.
Adsorption of proteins on Lignin?4 answersLignin has been found to adsorb proteins, such as glycinin and β-conglycinin, which are the main proteins in soy. The extent of adsorption is influenced by factors such as solution ionic strength and protein denaturation. The adsorption of undenatured proteins onto lignin is generally more extensive compared to denatured biomolecules, and a large amount of water is coupled to the adsorbed molecules. In the bioconversion of lignocellulosic substrates, the adsorption behavior of cellulase onto lignin negatively affects enzymatic hydrolysis of cellulose. Different lignin samples and components of cellulase mixtures exhibit different adsorption behaviors, with hydrophobic and electrostatic interactions playing important roles. Lignin derivatives, such as phenol and aminophenol derivatives, have been shown to adsorb proteinases and can be used as adsorbents for enzyme concentration or carriers for enzyme immobilization.
What biochemical processes involve proteins?5 answersProteins are involved in a variety of biochemical processes. They play a crucial role in catalytic acceleration of biochemical reactions by controlling the thermodynamics and kinetics involved. Proteins are also important for the structure and function of biological systems, and their energetics can be studied using techniques like high sensitivity differential scanning calorimetry (DSC). Enzymes, which are proteins, catalyze most biochemical processes and are regulated by the cells through inhibitors, activators, and altered gene expression. Additionally, proteins are involved in light-induced charge and energy transport in nucleic acids and proteins, which are fundamental to processes such as photosynthesis, vision, and DNA stability. Finally, proteins are being synthesized chemically to study the structural basis of biochemical activity, allowing for the construction of native proteins and their analogs.
How whey protein affects the colour of food?3 answersWhey protein has been found to affect the color of food. In a study by Sakata et al., it was observed that whey protein enzymatic hydrolysates, obtained by enzymatic treatment of whey protein concentrate (WPC), had a color-promoting effect on meat products. The hydrolysates, particularly the low molecular weight fractions, showed a higher color-promoting effect. Another study by Teba et al. investigated the influence of WPC on the physicochemical properties of rice-based extrudates and found that WPC increased redness and yellowness, while decreasing luminosity. The addition of WPC also improved the nutritional composition of the extrudates, especially proteins. These findings suggest that whey protein can enhance the color of food products and contribute to their overall appearance.
How does whey protein affect the Colour of food?3 answersWhey protein can affect the color of food by promoting color development and enhancing browning reactions. The enzymatic hydrolysate of whey protein, obtained through low-temperature sterilization and enzymatic digestion, has been found to have a similar color-promoting effect as L-ascorbic acid in sausages. Proteins in food can impact color and appearance, and processing can create alterations in proteins that result in changes in color. The addition of whey protein concentrate (WPC) to rice-based extrudates increased redness and yellowness while decreasing luminosity. The extrusion process positively affected the retention of polypeptide chains, improving the nutritional composition of the extrudates, especially proteins. Whey protein can interact with phenolic acids, altering the conformation of whey protein and affecting its color.