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  2. Ribbon diagram - Wikipedia

    en.wikipedia.org/wiki/Ribbon_diagram

    Ribbon diagram of myoglobin bound to haem (sticks) and oxygen (red spheres) (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 organisation of the protein backbone in 3D and ...

  3. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Knowing the structure of a similar homologous sequence (for example a member of the same protein family) allows highly accurate prediction of the tertiary structure by homology modeling. If the full-length protein sequence is available, it is possible to estimate its general biophysical properties, such as its isoelectric point.

  4. Protein topology - Wikipedia

    en.wikipedia.org/wiki/Protein_topology

    For example, two adjacent interacting alpha-helices or beta-strands can go in the same or in opposite directions. Topology diagrams of different proteins with known three-dimensional structure are provided by PDBsum ( an example ).

  5. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein dynamics and conformational changes allow proteins to function as nanoscale biological machines within cells, often in the form of multi-protein complexes. [14] Examples include motor proteins, such as myosin, which is responsible for muscle contraction, kinesin, which moves cargo inside cells away from the nucleus along microtubules ...

  6. Circuit topology - Wikipedia

    en.wikipedia.org/wiki/Circuit_topology

    This enabled topological analysis of proteins and genomes, which are often described as "unknot" in knot theory. [6] [7] Finally, circuit topology enables studying interactions between hard contacts and entanglements and can identify slip knots, while knot theory typically overlooks hard contacts and split knots. Thus, circuit topology serves ...

  7. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    The rough secondary-structure content of a biopolymer (e.g., "this protein is 40% α-helix and 20% β-sheet.") can be estimated spectroscopically. [15] For proteins, a common method is far-ultraviolet (far-UV, 170–250 nm) circular dichroism. A pronounced double minimum at 208 and 222 nm indicate α-helical structure, whereas a single minimum ...

  8. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    The image above contains clickable links This diagram (which is interactive) of protein structure uses PCNA as an example. (The tertiary structure of a protein consists of the way a polypeptide is formed of a complex molecular shape. This is caused by R-group interactions such as ionic and hydrogen bonds, disulphide bridges, and hydrophobic ...

  9. Ramachandran plot - Wikipedia

    en.wikipedia.org/wiki/Ramachandran_plot

    In biochemistry, a Ramachandran plot (also known as a Rama plot, a Ramachandran diagram or a [φ,ψ] plot), originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan, and V. Sasisekharan, [1] is a way to visualize energetically allowed regions for backbone dihedral angles ( also called as torsional angles , phi and psi angles ) ψ ...