Peptidomics, current status.
Characterisation of the complement of expressed proteins from a single genome is a central focus of the evolving field of proteomics. Traditional proteomics technologies were developed in the 20th century and are based on two-dimensional electrophoresis or multidimensional liquid chromatography. These facilitated functional genomics analysis, but they currently represent a significant bottleneck to progress in this area. We are now witnessing the development of novel alternative technologies for use in expression proteomics research. This review aims to familiarise the reader with the principles underlying the peptidomics approaches to proteomics research and provide examples of their applications.
Soloviev
Mikhail
M
School of Biological Sciences, Royal Holloway, University of London, Egham, Surrey, TW20 0EX, UK. mikhail.soloviev@rhul.ac.uk
Finch
Paul
P
D001120:Arginine / Q000737:chemistry; D002846:Chromatography, Affinity / Q000379:methods; D020650:Combinatorial Chemistry Techniques; D003545:Cysteine / Q000737:chemistry; D006639:Histidine / Q000737:chemistry; D006801:Humans; D008239:Lysine / Q000737:chemistry; D008715:Methionine / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D019000:Phosphotyrosine / Q000737:chemistry; D040901:Proteomics / Q000379:methods; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014364:Tryptophan / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry; D019010:Vascular Cell Adhesion Molecule-1 / Q000737:chemistry
D010455:Peptides; D019010:Vascular Cell Adhesion Molecule-1; D019000:Phosphotyrosine; D014443:Tyrosine; D006639:Histidine; D014364:Tryptophan; D001120:Arginine; D008715:Methionine; D008239:Lysine; D003545:Cysteine