Comput Biol Chem - Analysis of the relationships between evolvability, thermodynamics, and the functions of intrinsically disordered proteins/regions.

Tópicos

{ sequenc(1873) structur(1644) protein(1328) }
{ gene(2352) biolog(1181) express(1162) }
{ bind(1733) structur(1185) ligand(1036) }
{ analysi(2126) use(1163) compon(1037) }
{ import(1318) role(1303) understand(862) }
{ chang(1828) time(1643) increas(1301) }
{ research(1085) discuss(1038) issu(1018) }
{ studi(1119) effect(1106) posit(819) }
{ blood(1257) pressur(1144) flow(957) }
{ medic(1828) order(1363) alert(1069) }
{ sampl(1606) size(1419) use(1276) }
{ data(3008) multipl(1320) sourc(1022) }
{ studi(2440) review(1878) systemat(933) }
{ treatment(1704) effect(941) patient(846) }
{ algorithm(1844) comput(1787) effici(935) }
{ care(1570) inform(1187) nurs(1089) }
{ general(901) number(790) one(736) }
{ search(2224) databas(1162) retriev(909) }
{ system(1050) medic(1026) inform(1018) }
{ model(3480) simul(1196) paramet(876) }
{ data(2317) use(1299) case(1017) }
{ intervent(3218) particip(2042) group(1664) }
{ high(1669) rate(1365) level(1280) }
{ network(2748) neural(1063) input(814) }
{ take(945) account(800) differ(722) }
{ motion(1329) object(1292) video(1091) }
{ clinic(1479) use(1117) guidelin(835) }
{ extract(1171) text(1153) clinic(932) }
{ featur(1941) imag(1645) propos(1176) }
{ data(3963) clinic(1234) research(1004) }
{ model(2656) set(1616) predict(1553) }
{ group(2977) signific(1463) compar(1072) }
{ process(1125) use(805) approach(778) }
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{ can(774) often(719) complex(702) }
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{ method(1219) similar(1157) match(930) }
{ featur(3375) classif(2383) classifi(1994) }
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{ imag(2675) segment(2577) method(1081) }
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{ method(984) reconstruct(947) comput(926) }
{ case(1353) use(1143) diagnosi(1136) }
{ howev(809) still(633) remain(590) }
{ studi(1410) differ(1259) use(1210) }
{ risk(3053) factor(974) diseas(938) }
{ perform(999) metric(946) measur(919) }
{ model(2341) predict(2261) use(1141) }
{ visual(1396) interact(850) tool(830) }
{ compound(1573) activ(1297) structur(1058) }
{ perform(1367) use(1326) method(1137) }
{ spatial(1525) area(1432) region(1030) }
{ record(1888) medic(1808) patient(1693) }
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{ monitor(1329) mobil(1314) devic(1160) }
{ ehr(2073) health(1662) electron(1139) }
{ state(1844) use(1261) util(961) }
{ research(1218) medic(880) student(794) }
{ patient(2837) hospit(1953) medic(668) }
{ age(1611) year(1155) adult(843) }
{ signal(2180) analysi(812) frequenc(800) }
{ cost(1906) reduc(1198) effect(832) }
{ first(2504) two(1366) second(1323) }
{ activ(1138) subject(705) human(624) }
{ time(1939) patient(1703) rate(768) }
{ patient(1821) servic(1111) care(1106) }
{ use(2086) technolog(871) perceiv(783) }
{ can(981) present(881) function(850) }
{ health(1844) social(1437) communiti(874) }
{ structur(1116) can(940) graph(676) }
{ cancer(2502) breast(956) screen(824) }
{ use(976) code(926) identifi(902) }
{ use(1733) differ(960) four(931) }
{ drug(1928) target(777) effect(648) }
{ result(1111) use(1088) new(759) }
{ implement(1333) system(1263) develop(1122) }
{ survey(1388) particip(1329) question(1065) }
{ estim(2440) model(1874) function(577) }
{ decis(3086) make(1611) patient(1517) }
{ activ(1452) weight(1219) physic(1104) }
{ method(1969) cluster(1462) data(1082) }
{ method(2212) result(1239) propos(1039) }
{ detect(2391) sensit(1101) algorithm(908) }

Resumo

The evolvability of proteins is not only restricted by functional and structural importance, but also by other factors such as gene duplication, protein stability, and an organism's robustness. Recently, intrinsically disordered proteins (IDPs)/regions (IDRs) have been suggested to play a role in facilitating protein evolution. However, the mechanisms by which this occurs remain largely unknown. To address this, we have systematically analyzed the relationship between the evolvability, stability, and function of IDPs/IDRs. Evolutionary analysis shows that more recently emerged IDRs have higher evolutionary rates with more functional constraints relaxed (or experiencing more positive selection), and that this may have caused accelerated evolution in the flanking regions and in the whole protein. A systematic analysis of observed stability changes due to single amino acid mutations in IDRs and ordered regions shows that while most mutations induce a destabilizing effect in proteins, mutations in IDRs cause smaller stability changes than in ordered regions. The weaker impact of mutations in IDRs on protein stability may have advantages for protein evolvability in the gain of new functions. Interestingly, however, an analysis of functional motifs in the PROSITE and ELM databases showed that motifs in IDRs are more conserved, characterized by smaller entropy and lower evolutionary rate, than in ordered regions. This apparently opposing evolutionary effect may be partly due to the flexible nature of motifs in IDRs, which require some key amino acid residues to engage in tighter interactions with other molecules. Our study suggests that the unique conformational and thermodynamic characteristics of IDPs/IDRs play an important role in the evolvability of proteins to gain new functions.

Resumo Limpo

evolv protein restrict function structur import also factor gene duplic protein stabil organ robust recent intrins disord protein idpsregion idr suggest play role facilit protein evolut howev mechan occur remain larg unknown address systemat analyz relationship evolv stabil function idpsidr evolutionari analysi show recent emerg idr higher evolutionari rate function constraint relax experienc posit select may caus acceler evolut flank region whole protein systemat analysi observ stabil chang due singl amino acid mutat idr order region show mutat induc destabil effect protein mutat idr caus smaller stabil chang order region weaker impact mutat idr protein stabil may advantag protein evolv gain new function interest howev analysi function motif prosit elm databas show motif idr conserv character smaller entropi lower evolutionari rate order region appar oppos evolutionari effect may part due flexibl natur motif idr requir key amino acid residu engag tighter interact molecul studi suggest uniqu conform thermodynam characterist idpsidr play import role evolv protein gain new function

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