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Protein identification by peptide mass fingerprinting
1Finnigan MAT Ltd., Hemel Hempstead, UK.
Peptide Research
|May 1, 1994
Summary
Protein identification is achieved using mass spectrometry to analyze enzyme-digested peptide mixtures. This peptide mass fingerprinting technique accurately identifies proteins and their related sequences in databases.
Area of Science:
- Proteomics
- Biochemistry
- Bioinformatics
Background:
- Mass spectrometry generates specific peptide mass fingerprints from digested proteins.
- Protein identification can be achieved directly from these fingerprints.
Purpose of the Study:
- To review peptide mass fingerprinting techniques for protein identification.
- To compare database matching algorithms and discuss factors influencing accuracy.
Main Methods:
- Protein digestion with proteolytic enzymes (e.g., trypsin).
- Analysis of peptide mixtures using mass spectrometry (MALDI or ESI).
- Comparison of experimental mass values against sequence databases (e.g., SwissProt, PIR).
Main Results:
- Accurate protein identification possible from peptide mass fingerprints alone.
- Identification of homologous proteins when the exact protein is not in the database.
- Potential for identifying coding regions in genomic DNA.
Conclusions:
- Peptide mass fingerprinting is a powerful tool for protein identification and sequence homology analysis.
- Database matching algorithms and experimental factors are critical for accurate results.
- Inverted strategy shows promise for linking genomic DNA to expressed proteins.