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  2. Carbohydrate conformation - Wikipedia

    en.wikipedia.org/wiki/Carbohydrate_conformation

    The chair conformation of six-membered rings have a dihedral angle of 60° between adjacent substituents thus usually making it the most stable conformer. Since there are two possible chair conformation steric and stereoelectronic effects such as the anomeric effect, 1,3-diaxial interactions, dipoles and intramolecular hydrogen bonding must be taken into consideration when looking at relative ...

  3. 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.

  4. Haworth projection - Wikipedia

    en.wikipedia.org/wiki/Haworth_projection

    A Haworth projection has the following characteristics: [3] Carbon is the implicit type of atom. In the example on the right, the atoms numbered from 1 to 6 are all carbon atoms. Carbon 1 is known as the anomeric carbon. Hydrogen atoms on carbon are implicit. In the example, atoms 1 to 6 have extra hydrogen atoms not depicted.

  5. Structure validation - Wikipedia

    en.wikipedia.org/wiki/Structure_validation

    Structure validation concept: model of a protein (each ball is an atom), and magnified region with electron density data and 3 bright flags for problems. Macromolecular structure validation is the process of evaluating reliability for 3-dimensional atomic models of large biological molecules such as proteins and nucleic acids.

  6. Structural bioinformatics - Wikipedia

    en.wikipedia.org/wiki/Structural_bioinformatics

    Three-dimensional structure of a protein. Structural bioinformatics is the branch of bioinformatics that is related to the analysis and prediction of the three-dimensional structure of biological macromolecules such as proteins, RNA, and DNA. It deals with generalizations about macromolecular 3D structures such as comparisons of overall folds ...

  7. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. [1] The two most common secondary structural elements are alpha helices and beta sheets , though beta turns and omega loops occur as well.

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  9. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Quaternary structure is the three-dimensional structure consisting of the aggregation of two or more individual polypeptide chains (subunits) that operate as a single functional unit . The resulting multimer is stabilized by the same non-covalent interactions and disulfide bonds as in tertiary structure.