Protein peptide mass mapping

Proteomics of Protein Binders Peptide Mass Mapping Using Mass Spectrometry... 

This procedure is called Peptide Mass Mapping (PMM), which is defined as a means of protein identification by comparing observed masses (m/z values) with predicted masses of digested proteins contained in a database. 

Proteins fall into three classes when characterized with mass spectrometry proteins whose complete sequence is given in a database, proteins whose sequence is partially represented in expressed sequence tag databases, and proteins whose sequence is unknown. Proteins of the first class can be identified by peptide mass mapping in a very high through-... 

Even though the MALDI peptide mass mapping technique is very powerful, it has limitations. It requires well-separated proteins, is less sensitive than identifications based on electrospray tandem mass spectrometry, can only identify proteins whose complete sequences are available in databases, and does not produce redundant information. 

Yates JR, Speicher S, Griffin PR, Hunkapiller T. Peptide mass maps A highly informative approach to protein identification. Anal Biochem 1993 214(2) 397 408. 

Wilkins MR, Williams KL, Appel RD, Hochstrasser DF (1997) Proteome research new frontiers in functional genomics. Springer Verlag, Berlin Heidelberg Yates JR, Speicher S, Griffin PR, Hunkapiller T (1993) Peptide mass maps A highly informative approach to protein identification. Anal Biochem 214 397—408 Yates JR, Eng JK, McCormack AL, Schieltz D (1995) Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Analytical Chemistry 67 1426-1436. 

Tanaka, K., Takenaka, S., Tsuyama, S. and Wada, Y. (2006) Determination of unique amino acid substitutions in protein variants by peptide mass mapping with FT-ICR MS. 

The study of the proteome of the recombinant adenovirus type 5 vectors demonstrated an important apphcation of separation techniques in combination with MS methods in the drug discovery process. With completely sequenced adenovirus genome available, this approach provides a chemically well-dehned method of characterization of structural proteins of recombinant adenoviral vectors. The information of protein MWs, tryptic peptide mass mapping, and sequence tags of tryptic peptides derived from HPLC/MS resulted in the identification of 17 adenoviral proteins/polypeptides in the purified virion. The rapid and accurate identification of viral proteins from recombinant adenoviruses in this study is significant since it provides direct evidence of the maturation stage of adenoviruses, which is closely related to viral infectivity and efficacy in gene therapy. 

O.N. Jensen, A.V. Podtelejnikov, M. Mann, Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching. Anal. Chem., 69 (1997) 4741. 

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