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  2. Hydrophobic-polar protein folding model - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic-polar_protein...

    The hydrophobic-polar protein folding model is a highly simplified model for examining protein folds in space. First proposed by Ken Dill in 1985, it is the most known type of lattice protein: it stems from the observation that hydrophobic interactions between amino acid residues are the driving force for proteins folding into their native state. [1]

  3. Cloverleaf model of tRNA - Wikipedia

    en.wikipedia.org/wiki/Cloverleaf_model_of_tRNA

    For example, if the amino acid that attach to the end is phenylalanine, the reaction will be catalyzed by phenylalanine-tRNA synthase to produce tRNA phe. [ 4 ] The other end—the bottom often called the "DNA arm"—consists of a three base sequence that pairs with a complementary base sequence in a mRNA .

  4. Ribbon diagram - Wikipedia

    en.wikipedia.org/wiki/Ribbon_diagram

    Ribbon diagrams, also known as Richardson diagrams, are 3D schematic representations of protein structure and are one of the most common methods of protein depiction used today. The ribbon depicts the general course and organization of the protein backbone in 3D and serves as a visual framework for hanging details of the entire atomic structure ...

  5. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a

  6. File:L-amino acid structure.svg - Wikipedia

    en.wikipedia.org/.../File:L-amino_acid_structure.svg

    The following other wikis use this file: Usage on bn.wikipedia.org অ্যামিনো অ্যাসিড; Usage on en.wikiversity.org Organic Chemistry – Carbon Chemistry and Macromolecules

  7. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    The primary structure of a protein, its linear amino-acid sequence, determines its native conformation. [11] The specific amino acid residues and their position in the polypeptide chain are the determining factors for which portions of the protein fold closely together and form its three-dimensional conformation.

  8. Protein domain - Wikipedia

    en.wikipedia.org/wiki/Protein_domain

    The primary structure (string of amino acids) of a protein ultimately encodes its uniquely folded three-dimensional (3D) conformation. [20] The most important factor governing the folding of a protein into 3D structure is the distribution of polar and non-polar side chains. [21]

  9. 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] Only these 22 appear in the genetic code of life ...