Protein tertiary structure

Among the tertiary structure refers to the biochemistry of the parent spatial structure of proteins, nucleic acids or other macromolecules that are composed of a single chain. It is composed of several elements of the secondary structure and, as secondary structure is already encoded in the primary structure.

The parent of the tertiary structure is the quaternary structure. The hierarchical division into primary structure, secondary structure, tertiary structure and quaternary structure was proposed in 1952 by Kaj Ulrik Linderstrøm long.

Proteins

Particular proteins in the three-dimensional structure and the biological function characteristic is necessary. During or after the production of the protein by translation of an mRNA, the protein is converted by protein folding in the biologically active form. This process is i.a. supported by chaperones.

With a globular protein, the energetic driving force for the folding of the individual secondary structural elements is described by the Kautzman rule: the hydrophobic regions are in the interior, while the hydrophilic and / or charged areas facing the aqueous medium (see the hydrophobic effect). In the stabilization of tertiary structures disulfide bonds are involved ( weakest binding ) ( strongest binding ), ionic bonds, hydrogen bonds and hydrophobic interactions.

The next higher level is the quaternary structure.

Nucleic acids

Nucleic acids can also take complex spatial structures: tRNAs have for their function in the correct tertiary structure is involved.

Tertiary structure of a pseudoknot

Structure elucidation

The field of biochemistry, dealing with the Enlightenment and the impact of such structures, ie structural biology. As methods of structure determination are mainly used (X-ray ) Crystal structure analysis and multidimensional NMR. Bioinformatics methods and algorithms developed to predict the three-dimensional structure of the protein from its amino acid sequence ( primary structure).