The molar absorptivity of a protein in water at 280 nm can be estimated within ~5-10% from its content of the amino acids tyrosine and tryptophan and from the number of disulfide linkages (R-S-S-R) between cysteine residues: Ε280 nm (M-1 cm-1) ≈ 5500 nTrp + 1490 nTyr + 125 nS-S where nTrp is the number of tryptophans, nTyr is the number of tyrosines, and nS-S is the number of disulfide linkages. The protein human serum transferrin has 678 amino acids including 8 tryptophans, 26 tyrosines, and 19 disulfide linkages. The molecular mass of the most dominant for is 79550. Predict the molar absorptivity of transferrin. Predict the absorbance of a solution that’s 1.000 g/L transferrin in a 1.000-cm-pathlength cuvet. Estimate the g/L of a transferrin solution with an absorbance of 1.50 at 280 nm.
The molar absorptivity of a protein in water at 280 nm can be estimated within ~5-10% from its content of the amino acids tyrosine and tryptophan and from the number of disulfide linkages (R-S-S-R) between cysteine residues: Ε280 nm (M-1 cm-1) ≈ 5500 nTrp + 1490 nTyr + 125 nS-S where nTrp is the number of tryptophans, nTyr is the number of tyrosines, and nS-S is the number of disulfide linkages. The protein human serum transferrin has 678 amino acids including 8 tryptophans, 26 tyrosines, and 19 disulfide linkages. The molecular mass of the most dominant for is 79550. Predict the molar absorptivity of transferrin. Predict the absorbance of a solution that’s 1.000 g/L transferrin in a 1.000-cm-pathlength cuvet. Estimate the g/L of a transferrin solution with an absorbance of 1.50 at 280 nm.
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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- The molar absorptivity of a protein in water at 280 nm can be estimated within ~5-10% from its content of the amino acids tyrosine and tryptophan and from the number of disulfide linkages (R-S-S-R) between cysteine residues:
Ε280 nm (M-1 cm-1) ≈ 5500 nTrp + 1490 nTyr + 125 nS-S
where nTrp is the number of tryptophans, nTyr is the number of tyrosines, and nS-S is the number of disulfide linkages. The protein human serum transferrin has 678 amino acids including 8 tryptophans, 26 tyrosines, and 19 disulfide linkages. The molecular mass of the most dominant for is 79550.
- Predict the molar absorptivity of transferrin.
- Predict the absorbance of a solution that’s 1.000 g/L transferrin in a 1.000-cm-pathlength cuvet.
- Estimate the g/L of a transferrin solution with an absorbance of 1.50 at 280 nm.
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