Extinction Coefficient Equation:
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The extinction coefficient (ε) is a measure of how strongly a protein absorbs light at a specific wavelength, typically 280 nm. It depends on the number of aromatic amino acids (tryptophan, tyrosine) and cysteine residues in the protein structure.
The calculator uses the extinction coefficient equation:
Where:
Explanation: The equation calculates the theoretical extinction coefficient at 280 nm based on the protein's amino acid composition.
Details: The extinction coefficient is essential for protein quantification using UV spectrophotometry, determining protein concentration, and monitoring protein purification processes.
Tips: Enter the number of tryptophan, tyrosine, and cysteine residues in your protein. All values must be non-negative integers representing actual residue counts.
Q1: Why is extinction coefficient important?
A: It allows accurate protein concentration determination using UV absorbance at 280 nm without the need for standard curves.
Q2: What wavelength is used for protein extinction coefficient?
A: 280 nm is standard because aromatic amino acids (tryptophan and tyrosine) absorb strongly at this wavelength.
Q3: How accurate is this calculation?
A: This provides a theoretical estimate. Actual values may vary due to protein folding, solvent environment, and post-translational modifications.
Q4: Can I use this for modified proteins?
A: For proteins with significant modifications or non-standard chromophores, experimental determination is recommended.
Q5: What if my protein has no aromatic residues?
A: Proteins without tryptophan or tyrosine will have very low extinction coefficients and alternative quantification methods should be used.