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  2. Prochirality - Wikipedia

    en.wikipedia.org/wiki/Prochirality

    In stereochemistry, prochiral molecules are those that can be converted from achiral to chiral in a single step. [1] [2] An achiral species which can be converted to a chiral in two steps is called proprochiral. [2] If two identical substituents are attached to an sp 3-hybridized atom, the descriptors pro-R and pro-S are used to distinguish ...

  3. Chirality - Wikipedia

    en.wikipedia.org/wiki/Chirality

    Instead, both effects can also occur when the propagation direction of the electromagnetic wave together with the structure of an (achiral) material form a chiral experimental arrangement. [10] [11] This case, where the mutual arrangement of achiral components forms a chiral (experimental) arrangement, is known as extrinsic chirality. [12] [13]

  4. Non-proteinogenic amino acids - Wikipedia

    en.wikipedia.org/wiki/Non-proteinogenic_amino_acids

    Lysine. Technically, any organic compound with an amine (–NH 2) and a carboxylic acid (–COOH) functional group is an amino acid. The proteinogenic amino acids are a small subset of this group that possess a central carbon atom (α- or 2-) bearing an amino group, a carboxyl group, a side chain and an α-hydrogen levo conformation, with the exception of glycine, which is achiral, and proline ...

  5. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Proteins are often synthesized in an inactive precursor form; typically, an N-terminal or C-terminal segment blocks the active site of the protein, inhibiting its function. The protein is activated by cleaving off the inhibitory peptide. Some proteins even have the power to cleave themselves.

  6. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]

  7. Racemic crystallography - Wikipedia

    en.wikipedia.org/wiki/Racemic_crystallography

    Racemic crystal structure of Rv1738 from Mycobacterium tuberculosis produced by racemic protein crystallography. Racemic crystallography is a technique used in structural biology where crystals of a protein molecule are developed from an equimolar mixture of an L-protein molecule of natural chirality and its D-protein mirror image.

  8. Chirality (chemistry) - Wikipedia

    en.wikipedia.org/wiki/Chirality_(chemistry)

    An achiral molecule having chiral conformations could theoretically form a mixture of right-handed and left-handed crystals, as often happens with racemic mixtures of chiral molecules (see Chiral resolution#Spontaneous resolution and related specialized techniques), or as when achiral liquid silicon dioxide is cooled to the point of becoming ...

  9. Proline - Wikipedia

    en.wikipedia.org/wiki/Proline

    The exceptional conformational rigidity of proline affects the secondary structure of proteins near a proline residue and may account for proline's higher prevalence in the proteins of thermophilic organisms. Protein secondary structure can be described in terms of the dihedral angles φ, ψ and ω of the protein backbone. The cyclic structure ...