Protein Molecular Weight Calculator
Calculate average molecular mass for an unmodified linear peptide from its amino-acid sequence.
On this page
CalculatorHow to useFormula & methodWorked exampleWhy a sequence is not just a sum of free amino acidsKnow which chemical details are outside the sequenceFrequently asked questionsRelated calculatorsSourcesHow to use this calculator
- Enter the protein or peptide sequence using standard one-letter amino-acid codes. Spaces and line breaks are ignored.
- Set the number of identical separate chains if you want their combined mass.
- Read the average molecular mass in daltons and kilodaltons. The molar mass has the same numerical value in g/mol.
Formula and method
For the assumptions behind these results, read the explanation below. You can also explore Protein Concentration and DNA Concentration.
A worked example
Alanine plus glycine contribute 89.0935 + 75.0669 Da as free amino acids. Removing one water molecule for their peptide bond gives 146.1451 Da for the unmodified AG dipeptide.
Why a sequence is not just a sum of free amino acids
Amino acids join through peptide bonds. Each joining reaction removes the equivalent of one water molecule, so a linear chain with n residues has nβ1 peptide bonds. The first residue does not require a bond to a preceding residue. The correction therefore leaves the appropriate terminal groups in an unmodified, open chain.
The table used here contains average masses based on naturally occurring isotopes. These are different from monoisotopic masses commonly used in high-resolution mass spectrometry. Average-mass tables can differ slightly in their final digits because of the atomic weights and rounding used; the terminal-water convention is the same. Dalton and unified atomic mass unit are equivalent names for the molecular-scale unit; one kilodalton is one thousand daltons. Molar mass in grams per mole is numerically equivalent on this scale.
Know which chemical details are outside the sequence
The calculation assumes the 20 standard amino acids, unmodified termini, and a linear peptide. Disulfide bonds, phosphorylation, glycosylation, isotope labels, unusual residues, and other modifications change mass and are not inferred automatically. Do not compare a modified experimental species with this unmodified estimate without accounting for those differences.
Multiple separate identical chains are handled by multiplying each complete chainβs mass. No extra peptide bond is formed between those chains. If you want the mass of a single fused sequence, concatenate its residues and use one chain instead. Protein migration in a gel can also differ from ideal behavior, so this molecular-mass estimate alone does not guarantee an exact experimental band position.
Frequently asked questions
Can I paste a FASTA file?
Paste the sequence letters only, without the header line. Spaces and line breaks are accepted, but punctuation, stop symbols, and ambiguous residue codes are rejected.
Is this the mass of a charged ion?
No. It is the average neutral molecular mass. Mass-to-charge calculations require charge state and the relevant ion or adduct chemistry.
Sources and further reading
- University of Washington Proteomics Resource β Amino Acid Mass Table β
Distinguishes average and monoisotopic residue masses and explains adding terminal H and OH for a neutral linear chain. Last-digit differences can arise from the atomic weights and rounding used.
- OpenStax Chemistry 2e β Amines and Amides β
Explains peptide-bond formation and loss of one water molecule per bond, supporting the n β 1 water correction for an unmodified linear chain.
Our explanations are written for BiologyCalc. Read how we build and check our tools. These calculations are educational estimates where the underlying model requires assumptions.