ofcoz the protein migrate so long as it is charged ,once it become neutral it will stop migrating
To calculate the molecular weight of a protein in electrophoresis, you would use a standard curve generated with protein standards of known molecular weights run on the same gel. By plotting the migration distance of the standard proteins against their known molecular weights, you can then determine the molecular weight of your protein of interest based on its migration distance on the gel in comparison to the standard curve.
No. The reason is that low molecular weight compounds tend to have high molarity. As an example NaF is 42.5 molecular weight. So 42.5g dissolved in 1 liter of water would only be 4.25% but be 1 molar. Proteins tend to have every high molecular weight. So if a protein was say 1000 molecular weight, a 10% solution would contain 100g but only be 0.1 molar.
The human insulin protein is composed of 51 amino acids, and has a molecular mass of 5808 Da. Insulin for other species will be somewhat different.
Ebullioscopic method is a physiochemical method to determine the molecular weight of compounds....."when a non volatile solute is added to pure solvent or liquid the boiling point of the pure solvent is increased and the elevation in the temperature is related to the molecular weight of solute"this is given by formula:M=1000Kew/(ΔTW)WHERE Ke is the molal elevation constant,w is the weight of solute, W is the weight of solvent and M is the molecular weight................................................irfan ali bughio from uni of sindh,,,,,,,,,allama i.i qazi institute of chemistry..ayaan622@yahoo.com
In terms of molecular weight, proteins are generally heavier than sugars. Proteins are made up of long chains of amino acids, which have higher molecular weights compared to the simpler structures of sugars, which are carbohydrates. For example, a typical amino acid has a molecular weight around 110 daltons, while common sugars like glucose have a molecular weight of about 180 daltons. However, when comparing equal quantities by volume or mass, proteins will typically have a higher weight due to their complex structures.
To calculate the molecular weight of a protein in electrophoresis, you would use a standard curve generated with protein standards of known molecular weights run on the same gel. By plotting the migration distance of the standard proteins against their known molecular weights, you can then determine the molecular weight of your protein of interest based on its migration distance on the gel in comparison to the standard curve.
To determine the number of amino acids in your protein, you can use the average molecular weight of an amino acid which is about 110 Da (Daltons). By dividing the molecular weight of your protein (8.9 kD or 8900 Da) by the average weight of an amino acid (110 Da), you can estimate that your protein contains approximately 81 amino acids.
Proteins have the higher molecular weight. They consist of long chains of amino acids joined together.
The molecular weight of phosphorus (P) according to Dalton's method is approximately 31 g/mol.
Meyer's oscillating disc method is a technique used to determine the molecular weight of a polymer by measuring the change in weight of a solution containing the polymer as it oscillates at a specific frequency. This method allows for accurate determination of molecular weight and can be used to study the size and structure of macromolecules.
No. The reason is that low molecular weight compounds tend to have high molarity. As an example NaF is 42.5 molecular weight. So 42.5g dissolved in 1 liter of water would only be 4.25% but be 1 molar. Proteins tend to have every high molecular weight. So if a protein was say 1000 molecular weight, a 10% solution would contain 100g but only be 0.1 molar.
Haha wait are you in Amherst College biochemistry? What are the odds that 682 showed up on another college's problem set? Use 110 g/mol per amino acid (already corrected for the loss of water in amino acid condensation during formation of the protein) and multiply.
Its basically depends on weight of the body balancing with nitrogen gas of the body whcih balance sugar level.
In the formation of a peptide bond, a water molecule is "lost" (18Da), so if there are 100 amino acids (of average weight = 128), 99 peptide bonds were created, kicking out 99 x 18 = 162 Da. 100 AA x 128Da = 12,800 Dalton Removing the "water" upon condensation gives 12,800 Da - 162 Da = 12,638 Da = 12,638 g/mol
we can determine the molecular weight from landsberger experiment for elevation of boiling point by using the formula M2=(KBW2)*1000/T'W1 where M2=molecular mass Kb=ebullioscopic constant or molal boiling point constant W2=mass of solute W1=mass of solvent T'=change in temprature
The human insulin protein is composed of 51 amino acids, and has a molecular mass of 5808 Da. Insulin for other species will be somewhat different.
Ebullioscopic method is a physiochemical method to determine the molecular weight of compounds....."when a non volatile solute is added to pure solvent or liquid the boiling point of the pure solvent is increased and the elevation in the temperature is related to the molecular weight of solute"this is given by formula:M=1000Kew/(ΔTW)WHERE Ke is the molal elevation constant,w is the weight of solute, W is the weight of solvent and M is the molecular weight................................................irfan ali bughio from uni of sindh,,,,,,,,,allama i.i qazi institute of chemistry..ayaan622@yahoo.com