Protein identification by mass profile fingerprinting

Author(s): James P, Quadroni M, Carafoli E, Gonnet G


We have developed an algorithm for identifying proteins at the sub-microgram level without sequence determination by chemical degradation. The protein, usually isolated by one- or two-dimensional gel electrophoresis, is digested by enzymatic or chemical means and the masses of the resulting peptides are determined by mass spectrometry. The resulting mass profile, i.e., the list of the molecular masses of peptides produced by the digestion, serves as a fingerprint which uniquely defines a particular protein. This fingerprint may be used to search the database of known sequences to find proteins with a similar profile. If the protein is not yet sequenced the profile can serve as a unique marker. This provides a rapid and sensitive link between genomic sequences and 2D gel electrophoresis mapping of cellular proteins.

Similar Articles

Modular Peptide Synthetases Involved in Nonribosomal Peptide Synthesis

Author(s): Marahiel MA, Stachelhaus T, Mootz HD

Improving peptide fragmentation by N-terminal derivatization with high proton affinity

Author(s): Miyashita M, Hanai Y, Awane H, Yoshikawa T, Miyagawa H

Distortionless Enhancement of NMR Signalsby Polarization Transfer

Author(s): Doddrell DM, Pegg DT, Bendall MR


Author(s): http://www

Curtin-Hammett and steric effects in HOBt acylation regiochemistry

Author(s): Brink BD, DeFrancisco JR, Hillner JA, Linton BR

Termination of the structural confusion between plipastatin A1 and fengycin IX

Author(s): Honma M, Tanaka K, Konno K, Tsuge K, Okuno T, et al.