General three-dimensional form of local segments of proteins
This article is about secondary structure in protein. For the article about secondary structure in nucleic acid, see Nucleic acid secondary structure.
The image above contains clickable links This diagram (which is interactive) of protein structure uses PCNA as an example. (PDB: 1AXC)
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. Secondary structure elements typically spontaneously form as an intermediate before the protein folds into its three dimensional tertiary structure.
Secondary structure is formally defined by the pattern of hydrogen bonds between the amino hydrogen and carboxyl oxygen atoms in the peptide backbone. Secondary structure may alternatively be defined based on the regular pattern of backbone dihedral angles in a particular region of the Ramachandran plot regardless of whether it has the correct hydrogen bonds.
The concept of secondary structure was first introduced by Kaj Ulrik Linderstrøm-Lang at Stanford in 1952.[2][3] Other types of biopolymers such as nucleic acids also possess characteristic secondary structures.
^Sun PD, Foster CE, Boyington JC (May 2004). "Overview of protein structural and functional folds". Current Protocols in Protein Science. 17 (1): Unit 17.1. doi:10.1002/0471140864.ps1701s35. PMC 7162418. PMID 18429251.
^Linderstrøm-Lang KU (1952). Lane Medical Lectures: Proteins and Enzymes. Stanford University Press. p. 115. ASIN B0007J31SC.
^Schellman JA, Schellman CG (1997). "Kaj Ulrik Linderstrøm-Lang (1896–1959)". Protein Sci. 6 (5): 1092–100. doi:10.1002/pro.5560060516. PMC 2143695. PMID 9144781. He had already introduced the concepts of the primary, secondary, and tertiary structure of proteins in the third Lane Lecture (Linderstram-Lang, 1952)
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