Secondary structure in the context of Optical activity

Optical rotation, also known as polarization rotation or circular birefringence, is the rotation of the orientation of the plane of polarization about the optical axis of linearly polarized light as it travels through certain materials. Circular birefringence and circular dichroism are the manifestations of optical activity. Optical activity occurs only in chiral materials, those lacking microscopic mirror symmetry. Unlike other sources of birefringence which alter a beam's state of polarization, optical activity can be observed in fluids. This can include gases or solutions of chiral molecules such as sugars, molecules with helical secondary structure such as some proteins, and also chiral liquid crystals. It can also be observed in chiral solids such as certain crystals with a rotation between adjacent crystal planes (such as quartz) or metamaterials.

When looking at the source of light, the rotation of the plane of polarization may be either to the right (dextrorotatory or dextrorotary — d-rotary, represented by (+), clockwise), or to the left (levorotatory or levorotary — l-rotary, represented by (−), counter-clockwise) depending on which stereoisomer is dominant. For instance, sucrose and camphor are d-rotary whereas cholesterol is l-rotary. For a given substance, the angle by which the polarization of light of a specified wavelength is rotated is proportional to the path length through the material and (for a solution) proportional to its concentration.

In molecular biology, the collagen triple helix or type-2 helix is the main secondary structure of various types of fibrous collagen, including type I collagen. In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. Collagen folded into a triple helix is known as tropocollagen. Collagen triple helices are often bundled into fibrils which themselves form larger fibres, as in tendons.

Kaj Ulrik Linderstrøm-Lang (29 November 1896 – 25 May 1959) was a Danish protein scientist, who was the director of the Carlsberg Laboratory from 1939 until his death.

His most notable scientific contributions were the development of sundry physical techniques to study protein structure and function (especially hydrogen–deuterium exchange), and his definitions of protein primary, secondary, tertiary and quaternary structure.

In molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple, independent protein superfamilies (i.e. are not necessarily evolutionarily related to one another).