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What is the molar mass of haemocyanin and the freezing point of the solution when an aqueous solution is prepared by dissolving 1.5 grams of haemocyanin a protein obtained from crabs in 0.25 litres of?
Haemocyanins are a group of proteins.
What is the purpose of protein precipitation?
Removing protein from an aqueous solution does have its scientific significance; firstly, proteins can obstruct the measurement of other, smaller molecules within a solution and may these may need to be removed. However, more commonly, scientists may use this particular method as an early step in purifying a solution by separating the protein from a solution. An example of protein purification is commonly performed in the biotechnology industry where it is used to eradicate contaminants that are commonly contained in blood. Proteins can precipitate under certain circumstances without being unfolded and denatured. However, other agents may destroy the typical 3D structure of a protein; these agents wouldn't be used if protein precipitation was important as it usually disrupts the functionality of the protein.
Where would you expect to find serine and alanine in a globular protein in an aqueous solution?
Alanine is very hydrophobic as it is non-polar at its (medium sized) side chain. This means it will most often be found in the internal regions of a globular protein in an aqueous solution, as it will become buried during the hydrophobic collapse of the early stages of protein folding. There will be exceptions to this when the majority of amino acids near it in the polypeptide chain are hydrophilic. Serine has a polar hydroxyl group, making it slightly hydrophilic. You would therefore expect it to appear on the surface of the protein more often, or lining aqueous channels. It is only a little hydrophilic though, so it would not be surprising to find a more even distribution of serine around both the internal regions and external surfaces of the protein. More importantly though, the hydroxyl group of serine can be very reactive, particularly in certain environments produced by surrounding amino acids. Since it is very reactive, it is a common components of the catalytic (active) site of enzymes. For example, the catalytic triad of some protease enzymes.
How do you prepare 40 ml of a 2 mg ml protein solution from a 10mg ml protein solution?
You can prepare a 2 mg/ml protein solution by diluting the 10 mg/ml protein solution with a diluent in a 1:5 ratio. Measure 8 ml of the 10 mg/ml protein solution and add 32 ml of the diluent to make a total volume of 40 ml. Mix properly to ensure uniform distribution of the protein in the solution.
Why would you not use heat to kill microorganisms in a protein-rich solution?
You certainly can use heat to kill microorganisms in a "protein-rich" solution if you don't care whether the proteins get denatured or not.
Is ammonium sulfate aqueous?
No, by itself it is not. If dissolved in water it would then be aqueous.
What is the salt effect?
the low concentration of salt increases the protein solubility on aqueous solution,known as salting in effect
A series of hydrophobic side chains will congregate together as a protein folds in an aqueous solution and be stabilized by?
hydrophobic interactions. These interactions occur between nonpolar side chains, which are repelled by water and tend to come together to minimize exposure to the aqueous environment. This clustering leads to a decrease in entropy of water molecules surrounding the protein, contributing to the overall stability of the folded protein structure.
What is the molar mass of haemocyanin and the freezing point of the solution when an aqueous solution is prepared by dissolving 1.5 grams of haemocyanin a protein obtained from crabs in 0.25 litres of?
Haemocyanins are a group of proteins.
How does aqueous ammonium sulfate precipitate proteins?
Aqueous ammonium sulfate precipitates proteins by reducing the solubility of proteins in water. As the concentration of ammonium sulfate increases in the solution, it competes with the protein for water molecules, causing the protein to become less soluble and eventually precipitate out of the solution. This method is commonly used in protein purification techniques like salting out.
Are albumin and gelatin compact globular protein?
No
What is the purpose of protein precipitation?
Removing protein from an aqueous solution does have its scientific significance; firstly, proteins can obstruct the measurement of other, smaller molecules within a solution and may these may need to be removed. However, more commonly, scientists may use this particular method as an early step in purifying a solution by separating the protein from a solution. An example of protein purification is commonly performed in the biotechnology industry where it is used to eradicate contaminants that are commonly contained in blood. Proteins can precipitate under certain circumstances without being unfolded and denatured. However, other agents may destroy the typical 3D structure of a protein; these agents wouldn't be used if protein precipitation was important as it usually disrupts the functionality of the protein.
Where would you expect to find serine and alanine in a globular protein in an aqueous solution?
Alanine is very hydrophobic as it is non-polar at its (medium sized) side chain. This means it will most often be found in the internal regions of a globular protein in an aqueous solution, as it will become buried during the hydrophobic collapse of the early stages of protein folding. There will be exceptions to this when the majority of amino acids near it in the polypeptide chain are hydrophilic. Serine has a polar hydroxyl group, making it slightly hydrophilic. You would therefore expect it to appear on the surface of the protein more often, or lining aqueous channels. It is only a little hydrophilic though, so it would not be surprising to find a more even distribution of serine around both the internal regions and external surfaces of the protein. More importantly though, the hydroxyl group of serine can be very reactive, particularly in certain environments produced by surrounding amino acids. Since it is very reactive, it is a common components of the catalytic (active) site of enzymes. For example, the catalytic triad of some protease enzymes.
How do you prepare 40 ml of a 2 mg ml protein solution from a 10mg ml protein solution?
You can prepare a 2 mg/ml protein solution by diluting the 10 mg/ml protein solution with a diluent in a 1:5 ratio. Measure 8 ml of the 10 mg/ml protein solution and add 32 ml of the diluent to make a total volume of 40 ml. Mix properly to ensure uniform distribution of the protein in the solution.
What will be the effect of adding a concentrated urea solution to a protein?
denaturation of protein
What is the significance of the extinction coefficient of protein in determining its concentration in a solution?
The extinction coefficient of a protein is important because it helps determine the concentration of the protein in a solution. By measuring how much light is absorbed by the protein at a specific wavelength, the extinction coefficient can be used to calculate the concentration of the protein in the solution. This is valuable in various scientific experiments and analyses where knowing the precise concentration of a protein is crucial.
How does the precipitation of proteins occur with ammonium sulfate?
When ammonium sulfate is added to a protein solution, it disrupts the protein's structure by reducing the solubility of the protein. This causes the proteins to aggregate and precipitate out of the solution.
