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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).
A representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red).
Download QR code; Print/export Download as PDF; Printable version; ... Cell-free protein synthesis; Cephalodiscidae mitochondrial code; Chaperone (protein) Chemical ...
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. Proteins are made from amino acids. In humans, some amino acids can be synthesized using already existing intermediates. These amino ...
Glycosylphosphatidylinositol (pronunciation ⓘ) or glycophosphatidylinositol (GPI) is a phosphoglyceride that can be attached to the C-terminus of a protein during posttranslational modification. The resulting GPI-anchored proteins play key roles in a wide variety of biological processes. [ 1 ]
Amino acid activation (also known as aminoacylation or tRNA charging) refers to the attachment of an amino acid to its respective transfer RNA (tRNA). The reaction occurs in the cell cytosol and consists of two steps: first, the enzyme aminoacyl tRNA synthetase catalyzes the binding of adenosine triphosphate (ATP) to a corresponding amino acid, forming a reactive aminoacyl adenylate ...
mediates the entry of the aminoacyl tRNA into a free site of the ribosome. [4] EF-Ts: eEF-1B (β γ) [2] serves as the guanine nucleotide exchange factor for EF-Tu, catalyzing the release of GDP from EF-Tu. [2] EF-G: eEF-2: catalyzes the translocation of the tRNA and mRNA down the ribosome at the end of each round of polypeptide elongation.
Regulation of protein synthesis is partly influenced by phosphorylation of eIF2 (via the α subunit), which is a part of the eIF2-GTP-Met-tRNA i Met ternary complex (eIF2-TC). When large numbers of eIF2 are phosphorylated, protein synthesis is inhibited. This occurs under amino acid starvation or after viral infection.