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What is the substrate's of trypsin?
Trypsin is secreted by the duodenum (beginning of small intestine), where it breaks down peptides into amino acids, which helps the peptides (or proteins) better absorb into the intestines.
Do changes in salt concentration cause proteins to become denatured?
Yes, changes in salt concentration can denature proteins by disrupting the electrostatic interactions between charged amino acid residues. This can lead to unfolding and loss of protein structure and function.
What group of molecules are targeted by the kinases in order to control this movement?
Kinases target proteins, specifically enzymes, to regulate movement and cellular processes within the body. By phosphorylating specific amino acid residues on these target proteins, kinases can activate or inhibit their activity, leading to changes in cellular function and movement.
What insights can be gained from analyzing the glycine Ramachandran plot in protein structure prediction?
Analyzing the glycine Ramachandran plot in protein structure prediction can provide insights into the allowed conformations of glycine residues in proteins. This information can help in understanding the structural flexibility and stability of proteins, as well as in predicting their overall structure and function.
Are receptors and enzymes both located in the cell membrane?
Yes. There are many proteins embedded in the phospholipid bilayer. Some of these proteins are enzymes, and some are receptors; the receptors are glycoproteins, with short chains (oligosaccharides) of sugar residues attached to the protein. Other proteins act as means of transporting atoms, ions, and molecules across membranes (channel and carrier proteins).
Do proteins contain phosphorous?
Constitutively, proteins have no phosphorus as part of the molecule. However proteins can be phosphorylated by kinase enzymes that specifically add a phosphorus to certain amino acid residues, most of the times in Serine, Threonine or Tyrosine residues.
What is a multiresidue method?
A multiresidue method is an analytical technique used to detect and quantify multiple pesticide residues or contaminants in a single sample simultaneously. This method improves efficiency by allowing for the analysis of different residues in one test, making it a valuable tool for food safety and environmental monitoring.
What is the chemical equation for proteins?
Proteins have a very complicate chemical formula but not a "balanced chemical equation".
What is the function of beta mercaptoethanol?
It is used to reduce all disulfide bonds between cysteine residues in order to disrupt the tertiary and quaternary structures of proteins.
What breaks disulfide bonds in proteins?
Disulfide bonds in proteins are broken by reducing agents, such as dithiothreitol (DTT) or beta-mercaptoethanol. These agents break the sulfur-sulfur bonds in disulfide bonds, leading to the separation of the two cysteine residues involved.
Are all proteins more soluble in non polar solvents than in water?
No, not all proteins are more soluble in non-polar solvents than in water. The solubility of a protein depends on its structure and the nature of its amino acid residues. Some proteins are hydrophobic and have a higher solubility in non-polar solvents, while others are hydrophilic and have a higher solubility in water.
Why are residues hydrophobic in myoglobin but hydrophobic in hemoglobin?
Myoglobin and hemoglobin both contain hydrophobic residues, but their distributions and roles differ due to their functions and structures. In myoglobin, hydrophobic residues are primarily located within the interior of the protein, stabilizing its compact structure and facilitating oxygen binding. In hemoglobin, hydrophobic residues also contribute to the stability of the protein, but they play a crucial role in the cooperative binding of oxygen through interactions between subunits. Thus, while both proteins have hydrophobic residues, their specific arrangements and functional implications vary according to their distinct roles in oxygen transport and storage.
Why p53 is run as 53 kda on sds page?
p53 is detected as approximately 53 kDa on SDS-PAGE because it is a 53 kilodalton (kDa) protein. SDS-PAGE separates proteins based on size, so the molecular weight of p53 corresponds to the band observed at 53 kDa on the gel.
If Biuret and Millon's test give positive result what is the conclusion?
If both Biuret and Millon's tests give a positive result, it suggests the presence of proteins in the sample. Biuret test is specifically for proteins containing peptide bonds, while Millon's test is used for identifying proteins with tyrosine residues. The positive results from both tests provide strong evidence for the presence of proteins in the sample.
What vitamin is involved in carboxylation reactions?
Vitamin K is involved in carboxylation reactions, serving as a cofactor for enzymes that add carboxyl groups to specific proteins. This process is crucial for the activation of certain clotting factors and bone proteins.
What is the substrate's of trypsin?
Trypsin is secreted by the duodenum (beginning of small intestine), where it breaks down peptides into amino acids, which helps the peptides (or proteins) better absorb into the intestines.
What is role of sugar residues in the plasma membrane?
In bacteria they form the [cellulosic and exterior] Cell Wall; in animals sugars are combined with proteins to form the [exterior] Glyco-Calyx Cell Coat.
