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  2. Side chain - Wikipedia

    en.wikipedia.org/wiki/Side_chain

    Amino acids with similar polarity are usually attracted to each other, while nonpolar and polar side chains usually repel each other. Nonpolar/polar interactions can still play an important part in stabilizing the secondary structure due to the relatively large amount of them occurring throughout the protein. [ 6 ]

  3. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    For amino acids with charged side chains, the pK a of the side chain is involved. Thus for aspartate or glutamate with negative side chains, the terminal amino group is essentially entirely in the charged form −NH + 3 , but this positive charge needs to be balanced by the state with just one C-terminal carboxylate group is negatively charged.

  4. Beta sheet - Wikipedia

    en.wikipedia.org/wiki/Beta_sheet

    The side chains from the amino acid residues found in a β-sheet structure may also be arranged such that many of the adjacent sidechains on one side of the sheet are hydrophobic, while many of those adjacent to each other on the alternate side of the sheet are polar or charged (hydrophilic), [22] which can be useful if the sheet is to form a ...

  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. Proline - Wikipedia

    en.wikipedia.org/wiki/Proline

    Furthermore, proline is rarely found in α and β structures as it would reduce the stability of such structures, because its side chain α-nitrogen can only form one nitrogen bond. Additionally, proline is the only amino acid that does not form a red-purple colour when developed by spraying with ninhydrin for uses in chromatography. Proline ...

  7. Protein contact map - Wikipedia

    en.wikipedia.org/wiki/Protein_contact_map

    A protein contact map represents the distance between all possible amino acid residue pairs of a three-dimensional protein structure using a binary two-dimensional matrix. For two residues i {\displaystyle i} and j {\displaystyle j} , the i j {\displaystyle ij} element of the matrix is 1 if the two residues are closer than a predetermined ...

  8. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Amino acids are polymerised via peptide bonds to form a long backbone, with the different amino acid side chains protruding along it. In biological systems, proteins are produced during translation by a cell's ribosomes .

  9. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    The amino-acid side-chains are on the outside of the helix, and point roughly "downward" (i.e., toward the N-terminus), like the branches of an evergreen tree (Christmas tree effect). This directionality is sometimes used in preliminary, low-resolution electron-density maps to determine the direction of the protein backbone.