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  2. Histone H3 - Wikipedia

    en.wikipedia.org/wiki/Histone_H3

    The term "Histone H3" alone is purposely ambiguous in that it does not distinguish between sequence variants or modification state. Histone H3 is an important protein in the emerging field of epigenetics , where its sequence variants and variable modification states are thought to play a role in the dynamic and long term regulation of genes.

  3. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a ...

  4. Protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_structure_prediction

    the linear amino acid sequence of a protein, which chemically is a polypeptide chain composed of amino acids joined by peptide bonds. Profile (sequence context) a scoring matrix that represents a multiple sequence alignment of a protein family. The profile is usually obtained from a well-conserved region in a multiple sequence alignment.

  5. DNA and RNA codon tables - Wikipedia

    en.wikipedia.org/wiki/DNA_and_RNA_codon_tables

    A codon table can be used to translate a genetic code into a sequence of amino acids. [1] [2] The standard genetic code is traditionally represented as an RNA codon table, because when proteins are made in a cell by ribosomes, it is messenger RNA (mRNA) that directs protein synthesis. [2] [3] The mRNA sequence is determined by the sequence of ...

  6. 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]

  7. Protein fold class - Wikipedia

    en.wikipedia.org/wiki/Protein_fold_class

    Numerous protein structures are the result of rational design and do not exist in nature. Proteins can be designed from scratch (de novo design) or by making calculated variations on a known protein structure and its sequence (known as protein redesign). Rational protein design approaches make protein-sequence predictions that will fold to ...

  8. Walker motifs - Wikipedia

    en.wikipedia.org/wiki/Walker_motifs

    The Walker A and Walker B motifs are protein sequence motifs, known to have highly conserved three-dimensional structures. These were first reported in ATP-binding proteins by Walker and co-workers in 1982. [1] Of the two motifs, the A motif is the main "P-loop" responsible for binding phosphate, while the B motif is a much less conserved ...

  9. Helical wheel - Wikipedia

    en.wikipedia.org/wiki/Helical_wheel

    An example of an amino acid sequence plotted on a helical wheel. Aliphatic residues are shown as blue squares, polar or negatively charged residues as red diamonds, and positively charged residues as black octagons. A helical wheel is a type of plot or visual representation used to illustrate the properties of alpha helices in proteins.