Chirality and Handedness of Protein Structures View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2018-01

AUTHORS

A. V. Efimov

ABSTRACT

In proteins, the polypeptide chain forms a number of right- and left-handed helices and superhelices, right- and left-turned hairpins, and some other structures that are nonsuperimposable, although they are not mirror images of each other as the L-amino acids are not converted to the D-amino acids. This property of protein structures will be referred to here as pseudo-chirality - or handedness. It has been shown that there are two kinds of handedness in proteins - helical handedness and handedness of arrangement. Some protein structures exhibit both the kinds of handedness. Handedness is observed at all levels of protein structural organization - from α-helices, β-strands, hairpins, βαβ-units up to complex structural motifs, superhelices, and supramolecular structures in fibrous and polymer proteins. There are several structures that have unique handedness in proteins, for example, α-helices, αα-corners, βαβ-units, abcd-units, and so on. This property of the polypeptide chain is of particular value in protein folding and protein modeling, because it drastically reduces the number of possible folds. More... »

PAGES

s103-s110

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s0006297918140092

DOI

http://dx.doi.org/10.1134/s0006297918140092

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https://app.dimensions.ai/details/publication/pub.1101064470

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29544434


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