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  2. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    The side chains of the standard amino acids have a variety of chemical structures and properties, and it is the combined effect of all amino acids that determines its three-dimensional structure and chemical reactivity. [35] The amino acids in a polypeptide chain are linked by peptide bonds between amino and carboxyl

  3. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...

  4. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein structures range in size from tens to several thousand amino acids. [2] By physical size, proteins are classified as nanoparticles, between 1–100 nm. Very large protein complexes can be formed from protein subunits. For example, many thousands of actin molecules assemble into a microfilament.

  5. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Structure of a typical L-alpha-amino acid in the "neutral" form. Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2]

  6. Protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_structure_prediction

    The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns). The alignment of the H-bonds creates a dipole moment for the helix with a ...

  7. Protein (nutrient) - Wikipedia

    en.wikipedia.org/wiki/Protein_(nutrient)

    Absorption of the amino acids and their derivatives into which dietary protein is degraded is done by the gastrointestinal tract. The absorption rates of individual amino acids are highly dependent on the protein source; for example, the digestibilities of many amino acids in humans, the difference between soy and milk proteins [32] and between ...

  8. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    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 ...

  9. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    Modified amino acids are sometimes observed in proteins; this is usually the result of enzymatic modification after translation (protein synthesis). For example, phosphorylation of serine by kinases and dephosphorylation by phosphatases is an important control mechanism in the cell cycle .

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