Comput. Biol. Med. - A content and structural assessment of oxidative motifs across a diverse set of life forms.

Tópicos

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Resumo

Exposure to weightlessness (microgravity) or other protein stresses are detrimental to animal and human protein tissue health. Protein damage has been associated with stress and is linked to aging and the onset of diseases such as Alzheimers, Parkinsons, sepsis, and others. Protein stresses may cause alterations to physical protein structure, altering its functional identity. Alterations from stresses such as microgravity may be responsible for forms of muscle atrophy (as noted in returning astronauts), however, protein stresses come from other sources as well. Oxidative carbonylation is a protein stress which is a driving force behind protein decay and is attracted to protein segments enriched in R, K, P, T, E and S residues. Since mitochondria apply oxidative processes to produce ATP, their proteins may be placed in the same danger as those that are exposed to stresses. However, they do not appear to be impacted in the same way. Across 14 diverse organisms, we evaluate the coverage of motifs which are high in the amino acids thought to be affected by protein stresses such as oxidation. For this study, we study RKPT and PEST motifs which are both responsible for attracting forms of oxidation across mitochondrial and non-mitochondrial proteins. We show that mitochondrial proteins have fewer of these oxidative sites compared to non-mitochondrial proteins. Additionally, we analyze the oxidative regions to determine that their motifs preferentially tend to make up the connection points between the four kinds of structures of folded proteins (helices, turns, sheets, and coils).

Resumo Limpo

exposur weightless micrograv protein stress detriment anim human protein tissu health protein damag associ stress link age onset diseas alzheim parkinson sepsi other protein stress may caus alter physic protein structur alter function ident alter stress micrograv may respons form muscl atrophi note return astronaut howev protein stress come sourc well oxid carbonyl protein stress drive forc behind protein decay attract protein segment enrich r k p t e s residu sinc mitochondria appli oxid process produc atp protein may place danger expos stress howev appear impact way across divers organ evalu coverag motif high amino acid thought affect protein stress oxid studi studi rkpt pest motif respons attract form oxid across mitochondri nonmitochondri protein show mitochondri protein fewer oxid site compar nonmitochondri protein addit analyz oxid region determin motif preferenti tend make connect point four kind structur fold protein helic turn sheet coil

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