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Translation is one of the key energy consumers in cells, hence it is strictly regulated. Numerous mechanisms have evolved that control and regulate translation in eukaryotes as well as prokaryotes. Regulation of translation can impact the global rate of protein synthesis which is closely coupled to the metabolic and proliferative state of a cell.
The process of amino acid building to create protein in translation is a subject of various physic models for a long time starting from the first detailed kinetic models such as [26] or others taking into account stochastic aspects of translation and using computer simulations. Many chemical kinetics-based models of protein synthesis have been ...
Due to the fact that translation elongation is an irreversible process, there are few known mechanisms of its regulation. However, it has been shown that translational efficiency is reduced via diminished tRNA pools, which are required for the elongation of polypeptides.
A translation layer converts user interface controls in the language of a proteomics scientist to underlying complex informatics parameters. [18] Protein Prospector Open source: Protein Prospector is a package of about twenty proteomic analysis tools developed at the University of California San Francisco. The tandem mass spectrometry searching ...
The B protein is a flavin mononucleotide (FMN)-dependent dehydrogenase which oxidizes certain azoline rings into azoles. The B protein is typically referred to as the dehydrogenase; the C and D proteins together form the cyclodehydratase, although the D protein alone performs the cyclodehydration reaction. Early work on microcin B17 adopted a ...
Protein anabolism is the process by which proteins are formed from amino acids. It relies on five processes: amino acid synthesis, transcription , translation , post translational modifications , and protein folding .
Attachment of lipid molecules, known as lipidation, often targets a protein or part of a protein attached to the cell membrane. Other forms of post-translational modification consist of cleaving peptide bonds, as in processing a propeptide to a mature form or removing the initiator methionine residue.
The eIF2 alpha subunit is characterized by an OB-fold domain and two beta strands. This subunit helps to regulate translation, as it becomes phosphorylated to inhibit protein synthesis. [2] The eIF4F complex supports the cap-dependent translation initiation process and is composed of the initiation factors eIF4A, eIF4E, and eIF4G.