http://ru.wikipedia.org/wiki/Протеом

Протеом

Материал из Википедии — свободной энциклопедии

Протеом — термин для обозначения полного комплекта белков (протеинов), имеющихся в организме. Молекулы белков управляют всеми обменными процессами, протекающими в организме — пищеварением, выработкой гормонов или электрическим возбуждением нервных клеток и пр. Любые молекулярно-биологические процессы, происходящие в организме, отражаются в протеоме.

Термин был предложен в 1994 году австралийским исследователем Марком Уилкинсом.

Исследование протеома — крупный международный научный проект. В 2001 году для работы над ним была создана международная Организация протеома человека (Human Proteome Organization / HUPO). Особое внимание участников проекта вызывают белковые молекулы крови, печени и головного мозга.

Категории: Белки | Молекулярная биология

http://en.wikipedia.org/wiki/Proteome

Proteome

From Wikipedia, the free encyclopedia

The proteome is the entire complement of proteins expressed by a genome, cell, tissue or organism. More specifically, it is the set of expressed proteins at a given time under defined conditions. The term is a portmanteau of proteins and genome.

The term has been applied to several different types of biological systems. A cellular proteome is the collection of proteins found in a particular cell type under a particular set of environmental conditions such as exposure to hormone stimulation. It can also be useful to consider an organism's complete proteome, which can be conceptualized as the complete set of proteins from all of the various cellular proteomes. This is very roughly the protein equivalent of the genome. The term "proteome" has also been used to refer to the collection of proteins in certain sub-cellular biological systems. For example, all of the proteins in a virus can be called a viral proteome.

The proteome is larger than the genome, especially in eukaryotes, in the sense that there are more proteins than genes. This is due toalternative splicing of genes and post-translational modifications like glycosylation or phosphorylation.

Moreover the proteome has at least two levels of complexity lacking in the genome. When the genome is defined by the sequence ofnucleotides, the proteome cannot be limited to the sum of the sequences of the proteins present. Knowledge of the proteome requires knowledge of (1) the structure of the proteins in the proteome and (2) the functional interaction between the proteins.

Proteomics, the study of the proteome, has largely been practiced through the separation of proteins by two dimensional gel electrophoresis. In the first dimension, the proteins are separated by isoelectric focusing, which resolves proteins on the basis of charge. In the second dimension, proteins are separated by molecular weight using SDS-PAGE. The gel is dyed with Coomassie Blue or silver to visualize the proteins. Spots on the gel are proteins that have migrated to specific locations.

The mass spectrometer has augmented proteomics. Peptide mass fingerprinting identifies a protein by cleaving it into short peptides and then deduces the protein's identity by matching the observed peptide masses against a sequence database. Tandem mass spectrometry, on the other hand, can get sequence information from individual peptides by isolating them, colliding them with a non-reactive gas, and then cataloguing the fragment ions produced.

Categories: Proteomics | Bioinformatics | Proteins | Genomics