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.
A maker lane in electrophoresis is a designated lane in a gel where a molecular weight marker or ladder is run alongside the samples. This marker contains a mixture of DNA, RNA, or protein fragments of known sizes, allowing for the estimation of the sizes of the sample bands based on their position relative to the marker. It serves as a reference to help researchers determine the molecular weight of the unknown samples being analyzed.
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.
To determine the molecular weight of proteins separated by polyacrylamide gel electrophoresis (PAGE), a standard curve is created using known molecular weight standards run alongside the samples. After electrophoresis, the bands of the proteins are visualized and their migration distances are measured. By plotting the log of the molecular weights of the standards against their respective migration distances, you can interpolate the molecular weight of your unknown protein based on its migration distance. This method relies on the principle that smaller proteins migrate further through the gel compared to larger ones.
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.
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.
To calculate the molecular weight of a protein from blood, you typically use techniques like size-exclusion chromatography or SDS-PAGE to separate the proteins based on size. After separation, you can compare the migration distance of the protein of interest with standard proteins of known molecular weights. Additionally, you can use the protein's amino acid sequence, where the molecular weight is calculated by summing the average molecular weights of the individual amino acids and accounting for water molecules released during peptide bond formation. The final molecular weight can be expressed in Daltons (Da).
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.
A maker lane in electrophoresis is a designated lane in a gel where a molecular weight marker or ladder is run alongside the samples. This marker contains a mixture of DNA, RNA, or protein fragments of known sizes, allowing for the estimation of the sizes of the sample bands based on their position relative to the marker. It serves as a reference to help researchers determine the molecular weight of the unknown samples being analyzed.
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.
To determine the molecular weight of proteins separated by polyacrylamide gel electrophoresis (PAGE), a standard curve is created using known molecular weight standards run alongside the samples. After electrophoresis, the bands of the proteins are visualized and their migration distances are measured. By plotting the log of the molecular weights of the standards against their respective migration distances, you can interpolate the molecular weight of your unknown protein based on its migration distance. This method relies on the principle that smaller proteins migrate further through the gel compared to larger ones.
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