Latent Periodicity of Many Domains in Protein Sequences Reflects Their Structure, Function, and Evolution View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2004

AUTHORS

A. A. Laskin , E. V. Korotkov , N. A. Kudryashov

ABSTRACT

We have analyzed many protein sequences for the presence of latent periodicity common for their functionally identical sites. As a result, we found that Rossman-like domains of TPP-binding enzymes, ATP synthases, and pyridoxal phosphate-dependent enzymes as well as many other α/β-proteins, such as dethiobiotin synthases, have latently periodic structure. We also identified the periodicity pattern responsible for formation of parallel n-barrel in a number of enzymes. Possible relationships of regular structures and latent periodicity are also discussed. More... »

PAGES

135-143

Book

TITLE

Bioinformatics of Genome Regulation and Structure

ISBN

978-1-4757-4613-6
978-1-4419-7152-4

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4419-7152-4_14

DOI

http://dx.doi.org/10.1007/978-1-4419-7152-4_14

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042788799


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