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.
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© 2004 Springer Science+Business Media New York
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Laskin, A.A., Korotkov, E.V., Kudryashov, N.A. (2004). Latent Periodicity of Many Domains in Protein Sequences Reflects Their Structure, Function, and Evolution. In: Kolchanov, N., Hofestaedt, R. (eds) Bioinformatics of Genome Regulation and Structure. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-7152-4_14
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DOI: https://doi.org/10.1007/978-1-4419-7152-4_14
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-4613-6
Online ISBN: 978-1-4419-7152-4
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