Comput Biol Chem - Bacterial protein structures reveal phylum dependent divergence.

Tópicos

{ sequenc(1873) structur(1644) protein(1328) }
{ chang(1828) time(1643) increas(1301) }
{ cost(1906) reduc(1198) effect(832) }
{ problem(2511) optim(1539) algorithm(950) }
{ control(1307) perform(991) simul(935) }
{ howev(809) still(633) remain(590) }
{ survey(1388) particip(1329) question(1065) }
{ featur(3375) classif(2383) classifi(1994) }
{ take(945) account(800) differ(722) }
{ import(1318) role(1303) understand(862) }
{ signal(2180) analysi(812) frequenc(800) }
{ data(3008) multipl(1320) sourc(1022) }
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{ design(1359) user(1324) use(1319) }
{ general(901) number(790) one(736) }
{ data(3963) clinic(1234) research(1004) }
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{ state(1844) use(1261) util(961) }
{ group(2977) signific(1463) compar(1072) }
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{ age(1611) year(1155) adult(843) }
{ medic(1828) order(1363) alert(1069) }
{ gene(2352) biolog(1181) express(1162) }
{ first(2504) two(1366) second(1323) }
{ intervent(3218) particip(2042) group(1664) }
{ time(1939) patient(1703) rate(768) }
{ patient(1821) servic(1111) care(1106) }
{ can(981) present(881) function(850) }
{ analysi(2126) use(1163) compon(1037) }
{ health(1844) social(1437) communiti(874) }
{ structur(1116) can(940) graph(676) }
{ high(1669) rate(1365) level(1280) }
{ cancer(2502) breast(956) screen(824) }
{ use(976) code(926) identifi(902) }
{ use(1733) differ(960) four(931) }
{ drug(1928) target(777) effect(648) }
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{ estim(2440) model(1874) function(577) }
{ decis(3086) make(1611) patient(1517) }
{ process(1125) use(805) approach(778) }
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{ detect(2391) sensit(1101) algorithm(908) }

Resumo

Protein sequence space is vast compared to protein fold space. This raises important questions about how structures adapt to evolutionary changes in protein sequences. A growing trend is to regard protein fold space as a continuum rather than a series of discrete structures. From this perspective, homologous protein structures within the same functional classification should reveal a constant rate of structural drift relative to sequence changes. The clusters of orthologous groups (COG) classification system was used to annotate homologous bacterial protein structures in the Protein Data Bank (PDB). The structures and sequences of proteins within each COG were compared against each other to establish their relatedness. As expected, the analysis demonstrates a sharp structural divergence between the bacterial phyla Firmicutes and Proteobacteria. Additionally, each COG had a distinct sequence/structure relationship, indicating that different evolutionary pressures affect the degree of structural divergence. However, our analysis also shows the relative drift rate between sequence identity and structure divergence remains constant.

Resumo Limpo

protein sequenc space vast compar protein fold space rais import question structur adapt evolutionari chang protein sequenc grow trend regard protein fold space continuum rather seri discret structur perspect homolog protein structur within function classif reveal constant rate structur drift relat sequenc chang cluster ortholog group cog classif system use annot homolog bacteri protein structur protein data bank pdb structur sequenc protein within cog compar establish related expect analysi demonstr sharp structur diverg bacteri phyla firmicut proteobacteria addit cog distinct sequencestructur relationship indic differ evolutionari pressur affect degre structur diverg howev analysi also show relat drift rate sequenc ident structur diverg remain constant

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