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  2. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    In a hydrophilic environment such as cytosol, the hydrophobic amino acids will concentrate at the core of the protein, while the hydrophilic amino acids will be on the exterior. This is entropically favorable since water molecules can move much more freely around hydrophilic amino acids than hydrophobic amino acids.

  3. Translation (biology) - Wikipedia

    en.wikipedia.org/wiki/Translation_(biology)

    Overview of eukaryotic messenger RNA (mRNA) translation Translation of mRNA and ribosomal protein synthesis Initiation and elongation stages of translation involving RNA nucleobases, the ribosome, transfer RNA, and amino acids The three phases of translation: (1) in initiation, the small ribosomal subunit binds to the RNA strand and the initiator tRNA–amino acid complex binds to the start ...

  4. Eukaryotic translation - Wikipedia

    en.wikipedia.org/wiki/Eukaryotic_translation

    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.

  5. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    The folding of many proteins begins even during the translation of the polypeptide chain. The amino acids interact with each other to produce a well-defined three-dimensional structure, known as the protein's native state. This structure is determined by the amino-acid sequence or primary structure. [2]

  6. Ribosomally synthesized and post-translationally modified ...

    en.wikipedia.org/wiki/Ribosomally_synthesized...

    They are a member of a larger class of amino-acid-based lasso structures. Additionally, lasso peptides are formally rotaxanes. The N-terminal "ring" can be from 7 to 9 amino acids long and is formed by an isopeptide bond between the N-terminal amine of the first amino acid of the peptide and the carboxylate side chain of an aspartate or ...

  7. Ribosome - Wikipedia

    en.wikipedia.org/wiki/Ribosome

    Amino acids are selected and carried to the ribosome by transfer RNA (tRNA) molecules, which enter the ribosome and bind to the messenger RNA chain via an anticodon stem loop. For each coding triplet in the messenger RNA, there is a unique transfer RNA that must have the exact anti-codon match, and carries the correct amino acid for ...

  8. Post-translational modification - Wikipedia

    en.wikipedia.org/wiki/Post-translational...

    Post-translational modifications can occur on the amino acid side chains or at the protein's C-or N-termini. [1] They can expand the chemical set of the 22 amino acids by changing an existing functional group or adding a new one such as phosphate.

  9. Ribosomal pause - Wikipedia

    en.wikipedia.org/wiki/Ribosomal_pause

    Ribosomal pause refers to the queueing or stacking of ribosomes during translation of the nucleotide sequence of mRNA transcripts. These transcripts are decoded and converted into an amino acid sequence during protein synthesis by ribosomes. Due to the pause sites of some mRNA's, there is a disturbance caused in translation. [1]