Peptide mass map

It should be pointed out that FAB, MALDI, and ESI can be used to provide ions for peptide mass maps or for microsequencing and that any kind of ion analyzer can support searches based only on molecular masses. Fragment or sequence ions are provided by instruments that can both select precursor ions and record their fragmentation. Such mass spectrometers include ion traps, Fourier transform ion cyclotron resonance, tandem quadrupole, tandem magnetic sector, several configurations of time-of-flight (TOF) analyzers, and hybrid systems such as quadrupole-TOF and ion trap-TOF analyzers. 

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. 

Table 6.2 The most often used endopeptidases in peptide mass mapping...

Table 6.6 Identification of the proteinaceous binders in the model mortar samples by peptide mass mapping [32]... 

Peterson DS, Rohr T, Svec FK, Frechet JMJ (2003) Dual-function microanalyt-ical device by in situ photolithographic grafting of porous polymer monolith integrating solid-phase extraction and enzymatic digestion for peptide mass mapping. Anal Chem 75 5328... 

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. 

Laugesen, S. Roepstoiff, P. Combination of Two Matrices Results in Improved Performance of Maldi MS for Peptide Mass Mapping and Protdn Analysis. J. Am. Soc. 

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. 

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