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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 ...
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 translation machinery works relatively slowly compared to the enzyme systems that catalyze DNA replication. Proteins in bacteria are synthesized at a rate of only 18 amino acid residues per second, whereas bacterial replisomes synthesize DNA at a rate of 1000 nucleotides per second.
Protein synthesis is a very similar process for both prokaryotes and eukaryotes but there are some distinct differences. [1] Protein synthesis can be divided broadly into two phases: transcription and translation. During transcription, a section of DNA encoding a protein, known as a gene, is converted into a molecule called messenger RNA (mRNA).
They serve critical roles in forming the catalytic sites of translation of mRNA. During translation of mRNA, rRNA functions to bind both mRNA and tRNA to facilitate the process of translating mRNA's codon sequence into amino acids. rRNA initiates the catalysis of protein synthesis when tRNA is sandwiched between the SSU and LSU.
Each codon codes for a specific amino acid, except the stop codons, which terminate protein synthesis. The translation of codons into amino acids requires two other types of RNA: transfer RNA, which recognizes the codon and provides the corresponding amino acid, and ribosomal RNA (rRNA), the central component of the ribosome's protein ...
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.
Then the protein passes through the golgi apparatus, where it is packaged into a vesicle. In the vesicle, more parts are cut off, and it turns into mature insulin. In molecular biology, post-translational modification (PTM) is the covalent process of changing proteins following protein biosynthesis. PTMs may involve enzymes or occur spontaneously.