Extinction Coefficient Formula:
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The molar extinction coefficient (ε) measures how strongly a chemical species absorbs light at a given wavelength. For peptides, it's calculated from the sum of contributions from individual amino acids, particularly tryptophan, tyrosine, and cysteine residues.
The calculator uses the extinction coefficient formula:
Where:
Standard Values:
Details: The extinction coefficient is essential for quantifying protein concentration using UV spectrophotometry, determining protein purity, and studying protein-ligand interactions.
Tips: Select the amino acid type, enter the number of residues, and add any necessary correction factors. The calculator will compute the total extinction coefficient at 280 nm.
Q1: Why are only three amino acids considered?
A: Tryptophan, tyrosine, and cysteine are the primary amino acids that absorb significantly at 280 nm, which is the standard wavelength for protein quantification.
Q2: What are typical extinction coefficient values?
A: For most proteins, extinction coefficients range from 10,000 to 100,000 M⁻¹ cm⁻¹, depending on the number of aromatic residues.
Q3: When are correction factors needed?
A: Correction factors account for disulfide bonds, unusual amino acid modifications, or specific buffer conditions that may affect absorbance.
Q4: How accurate is this calculation?
A: This provides a theoretical estimate. For precise work, experimental determination is recommended, especially for proteins with unusual structures.
Q5: Can this be used for protein concentration calculation?
A: Yes, once you have the extinction coefficient, you can calculate protein concentration using Beer-Lambert law: Concentration = Absorbance / (ε × path length).