Tertiary structure

From WikiMD's Food, Medicine & Wellness Encyclopedia

Tertiary structure refers to the three-dimensional structure of a protein or nucleic acid molecule. It is the third level of protein structure and is the overall spatial arrangement of atoms in a protein. Tertiary structure is primarily due to interactions between the R groups of the amino acids that make up the protein.

Overview[edit | edit source]

Tertiary structure is determined by a variety of non-covalent interactions, like hydrophobic interactions, ionic bonding, hydrogen bonding, and Van der Waals forces, as well as by disulfide bonds. These interactions tend to bend and twist the protein into a variety of conformations. However, there is usually a single stable conformation that is most energetically favorable, which the protein folds into spontaneously.

Determination of Tertiary Structure[edit | edit source]

The tertiary structure of a protein can be determined using a variety of experimental techniques, such as X-ray crystallography, NMR spectroscopy, and cryo-electron microscopy. These techniques allow the positions of the individual atoms within the protein to be measured in relation to each other, revealing the three-dimensional structure of the protein.

Importance of Tertiary Structure[edit | edit source]

The tertiary structure of a protein is critical for its function. For example, the tertiary structure of enzymes allows them to bind to their substrates and carry out their catalytic functions. Changes in the tertiary structure can result in loss of function and can lead to diseases such as Alzheimer's disease and sickle cell anemia.

See Also[edit | edit source]

Tertiary structure Resources
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