Proteins protein identification

D. Eigeys, Y. Zhang and R. Aebersold, Optimization of solid phase microexti action-capillaiy zone electi ophoresis-mass specti ometi y for liigh sensitivity protein identification , Electrophoresis 19 2338-2347 (1998). 

D. Eigeys, A. Dua et, J. R. Yates-III and R. Aebersold, Protein identification by solid phase microextraaion-capillaiy zone electi ophoi esis-miaoelecti ospray-tandem mass specti ometi y , Nat. Biotechnol. 14 1579-1583 (1996). 

Peptide mass fingeiprinting (PMF) is a mass spectrometry based method for protein identification. The protein is cleaved by an enzyme with high specificity (trypsin, Lys-C, Asp-N, etc.) or chemical (CNBr). The peptide mixture generated is analyzed by matrix-assisted laser desorp-tion/ionization (MALDI) or electrospray ionization (ESI)... 

Wilkins MR et al (1996) From proteins to proteomes large scale protein identification by two-dimensional electrophoresis and amino acid analysis. BioTechnol 14 61-65... 

Bochicchio, B. and Tamburro, A.M., Polyproline II structure in proteins Identification by chiroptical spectroscopies, stability, and functions. Chirality, 14(10), 782-792, 2002. 

Geveart K, Vandekerckhove J Protein identification methods in proteomics. Electrophoresis 2000 21 1145. 

Holz A, Bielekova B, Martin R, Oldstone MB (2000) MyeUn-assodated oUgodendrocytic basic protein identification of an encephafitogenic epitope and association with multiple sclerosis. J Immunol 164 1103-1109... 

Griffiths, H.R, Lunec, J. and Blake, D.R. (1992). Oxygen radical-induced fluorescence in proteins identification of the fluorescent tryptophan metabolite N formyl kynurenine as a biological index of radical damage. Amino Acids 3, 183-194. 

The ability to visualize spots on a 2D gel, while useful as a fingerprint, is not the same as protein identification. Protein sequencing by the Edman degradation technique is the classical means of determining... 

Tandem mass spectrometry (MS/MS) is another common approach used for protein identification. In this method, proteins are digested and the resulting peptides are ionized directly from the liquid phase by... 

The experiments described above indicate that technology is available to couple SPR with mass spectrometry. These methods should be useful for protein-protein interaction mapping. For example, immobilized proteins can be used as hooks for fishing binding partners from complex protein mixtures under native conditions. The coupling of techniques can lead not only to the rapid identification of interacting proteins but will also provide information on the kinetic parameters of the interaction. This approach should serve as an excellent complement to the use of in vivo techniques such as the yeast two-hybrid system. 

Bemdt, P., Hobohm, U., and Langen, H. (1999). Reliable automatic protein identification from matrix-assisted laser desorption/ionization mass spectrometric peptide fingerprints. Electrophoresis 20, 3521-3526. 

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