Latent periodicity of serine-threonine and tyrosine protein kinases and another protein families

dc.creatorLaskin, Andrew A.
dc.creatorKudryashov, Nikolai A.
dc.creatorSkryabin, Konstantin G.
dc.creatorKorotkov, Eugene V.
dc.date2004-09-06
dc.date.accessioned2026-07-07T05:58:37Z
dc.date.available2026-07-07T05:58:37Z
dc.descriptionWe identified latent periodicity in catalytic domains of approximately 85% of serine/threonine and tyrosine protein kinases. Similar results were obtained for other 22 protein domains. We also designed the method of noise decomposition, which is aimed to distinguish between different periodicity types of the same period length. The method is to be used in conjunction with the cyclic profile alignment, and this combination is able to reveal structure-related or function-related patterns of latent periodicity. Possible origins of the periodic structure of protein kinase active sites are discussed. Summarizing, we presume that latent periodicity is the common property of many catalytic protein domains.
dc.description27 pages, 3 figures, 6 tables, 57 references
dc.identifierhttps://arxiv.org/abs/q-bio/0409008
dc.identifierhttp://arxiv.org/abs/q-bio/0409008
dc.identifierMolekularnuya Biologiya (Russian), vol.39, N3, 2005
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/88424
dc.subjectBiomolecules
dc.titleLatent periodicity of serine-threonine and tyrosine protein kinases and another protein families
dc.typetext

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