. "Um alinhamento estrutural \u00E9 um tipo de alinhamento de sequ\u00EAncias baseado na compara\u00E7\u00E3o da forma das mol\u00E9culas. Estes alinhamentos tentam estabelecer equival\u00EAncias entre duas ou mais estruturas de pol\u00EDmeros baseando-se na sua forma e . O processo normalmente aplica-se \u00E0s das prote\u00EDnas, mas tamb\u00E9m pode ser usado para longas mol\u00E9culas de RNA. Ao contr\u00E1rio da sobreposi\u00E7\u00E3o estrutural simples, onde se conhecem alguns res\u00EDduos equivalentes das duas estruturas, o alinhamento estrutural n\u00E3o requer um conhecimento pr\u00E9vio de posi\u00E7\u00F5es equivalentes. \u00C9 uma valiosa ferramenta para a compara\u00E7\u00E3o de prote\u00EDnas que t\u00EAm poucas semelhan\u00E7as entre as suas sequ\u00EAncias, onde as rela\u00E7\u00F5es evolutivas entre prote\u00EDnas n\u00E3o podem ser facilmente detectadas por t\u00E9cnicas padr\u00E3o de alinhamento de seq\u00FC\u00EAncias. Portanto, o alinhamento estrutural pode ser utilizado para sugerir rela\u00E7\u00F5es evolutivas entre prote\u00EDnas que compartilham uma sequ\u00EAncia comum muito curta. Por\u00E9m, o uso dos resultados como evid\u00EAncia dum antepassado evolutivo comum deve ser feito com cautela, dado os poss\u00EDveis efeitos da confus\u00E3o com a evolu\u00E7\u00E3o convergente, segundo a qual m\u00FAltiplas sequ\u00EAncias de amino\u00E1cidos sem rela\u00E7\u00E3o filogen\u00E9tica entre eles convergem originando uma mesma estrutura terci\u00E1ria. Os alinhamentos estruturais podem comparar duas ou m\u00FAltiplas sequ\u00EAncias. Como estes alinhamentos dependem da informa\u00E7\u00E3o sobre todas as conforma\u00E7\u00F5es tridimensionais das sequ\u00EAncias do problema, o m\u00E9todo s\u00F3 pode ser usado para seq\u00FC\u00EAncias onde essas estruturas sejam conhecidas. Estes encontram-se normalmente por cristalografia de raios X ou espectroscopia de resson\u00E2ncia magn\u00E9tica nuclear. \u00C9 poss\u00EDvel realizar um alinhamento estrutural de estruturas produzidas por m\u00E9todos de . Para a avalia\u00E7\u00E3o destas previs\u00F5es, muitas vezes \u00E9 necess\u00E1rio fazer um alinhamento estrutural entre o modelo e a estrutura real conhecida para avaliar a qualidade do modelo. Os alinhamentos estruturais s\u00E3o especialmente \u00FAteis para analisar dados surgidos dos campos da gen\u00F3mica estrutural e da prote\u00F3mica, e podem ser utilizados como pontos de compara\u00E7\u00E3o para avaliar alinhamentos gerados por m\u00E9todos bioinform\u00E1ticos baseados exclusivamente em sequ\u00EAncias. O resultado dum alinhamento estrutural \u00E9 uma superposi\u00E7\u00E3o dos conjuntos de coordenadas at\u00F3micas, e uma dist\u00E2ncia m\u00EDnima (ou RMSD, acr\u00F3nimo de Root Mean Square Deviation, ou ) entre as estruturas b\u00E1sicas das prote\u00EDnas sobrepostas. A RMSD de estruturas alinhadas indica as diverg\u00EAncias entre elas. O alinhamento estrutural pode complicar-se pela exist\u00EAncia de m\u00FAltiplos no interior duma ou mais estruturas de entrada (input), uma vez que altera\u00E7\u00F5es na orienta\u00E7\u00E3o relativa dos dom\u00EDnios entre duas estruturas a alinhar podem exagerar para RMSD artificialmente."@pt . . . . . . . . . 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\u043F\u043E\u043B\u0443\u0447\u0435\u043D\u043D\u044B\u0445 \u043F\u0443\u0442\u0451\u043C \u0441\u0440\u0430\u0432\u043D\u0435\u043D\u0438\u044F \u043F\u043E\u0441\u043B\u0435\u0434\u043E\u0432\u0430\u0442\u0435\u043B\u044C\u043D\u043E\u0441\u0442\u0435\u0439."@ru . "1998-12-03"^^ . "Structural alignment"@en . . . . . . . "Strukturn\u00ED alignment je zp\u016Fsob porovn\u00E1v\u00E1n\u00ED polymern\u00EDch struktur na z\u00E1klad\u011B jejich tvaru a prostorov\u00E9ho rozlo\u017Een\u00ED. Krom\u011B ur\u010Dov\u00E1n\u00ED podobnost\u00ED protein\u016F nach\u00E1z\u00ED vyu\u017Eit\u00ED i p\u0159i porovn\u00E1v\u00E1n\u00ED molekul RNA. Ur\u010Den\u00ED podobnosti protein\u016F pat\u0159\u00ED mezi d\u016Fle\u017Eit\u00E9 faktory spr\u00E1vn\u00E9 klasifikace protein\u016F, ze strukturn\u00ED podobnosti s ostatn\u00EDmi proteiny lze vyvodit informace o evolu\u010Dn\u00EDm v\u00FDvoji, nebo biologick\u00E9 funkci, \u010Deho\u017E se vyu\u017E\u00EDv\u00E1 nap\u0159. p\u0159i klasifikaci nov\u011B objeven\u00FDch protein\u016F, u kter\u00FDch je zn\u00E1ma pouze struktura. Pro strukturn\u00ED alignment nen\u00ED pot\u0159eba p\u0159edem zn\u00E1t informace o spole\u010Dn\u00FDch oblastech protein\u016F. V p\u0159\u00EDpad\u011B, \u017Ee maj\u00ED proteiny velkou sekven\u010Dn\u00ED podobnost, vyu\u017E\u00EDv\u00E1 se sp\u00ED\u0161e sekven\u010Dn\u00ED alignment nam\u00EDsto strukturn\u00EDho."@cs . . . . . . . . "474908"^^ . . "\u062A\u0631\u0627\u0635\u0641 \u0628\u0646\u064A\u0648\u064A"@ar . . . . . . . . . "Strukturn\u00ED alignment"@cs . . . . . . "Un alineamiento estructural es un tipo de alineamiento de secuencias basado en la comparaci\u00F3n de la forma. Estos alineamientos intentan establecer equivalencias entre dos o m\u00E1s estructuras de pol\u00EDmeros bas\u00E1ndose en su forma y conformaci\u00F3n tridimensional. El proceso se aplica normalmente a las estructuras terciarias de las prote\u00EDnas, pero tambi\u00E9n puede usarse para largas mol\u00E9culas de ARN. En contraste a la simple superposici\u00F3n estructural, donde al menos se conocen algunos residuos equivalentes de las dos estructuras, el alineamiento estructural no requiere un conocimiento previo de posiciones equivalentes. Es una valiosa herramienta para la comparaci\u00F3n de prote\u00EDnas con baja similitud entre sus secuencias, en donde las relaciones evolutivas entre prote\u00EDnas no pueden ser f\u00E1cilmente detectadas por t\u00E9cnicas est\u00E1ndares de alineamiento de secuencias. El alineamiento estructural puede usarse, por lo tanto, para sugerir relaciones evolutivas entre prote\u00EDnas que comparten una secuencia com\u00FAn muy corta. Sin embargo, el uso de los resultados como evidencia de un ancestro evolutivo com\u00FAn debe realizarse con cautela dados los posibles efectos de confusi\u00F3n con la evoluci\u00F3n convergente, seg\u00FAn la cual m\u00FAltiples secuencias de amino\u00E1cidos sin relaci\u00F3n filogen\u00E9tica entre s\u00ED convergen a una misma estructura terciaria. Los alineamientos estructurales pueden comparar dos o m\u00FAltiples secuencias. Puesto que estos alineamientos dependen de informaci\u00F3n sobre todas las conformaciones tridimensionales de las secuencias problema, el m\u00E9todo solo puede ser usado sobre secuencias donde estas estructuras sean conocidas. Estas se encuentran normalmente por cristalograf\u00EDa de rayos X o espectroscopia de resonancia magn\u00E9tica nuclear. Es posible realizar un alineamiento estructural sobre estructuras producidas mediante m\u00E9todos de predicci\u00F3n de estructura. En efecto, la evaluaci\u00F3n de tales predicciones requiere a menudo un alineamiento estructural entre el modelo y la estructura real conocida para evaluar la calidad del modelo. Los alineamientos estructurales son especialmente \u00FAtiles para analizar datos surgidos de los campos de la gen\u00F3mica estructural y de la prote\u00F3mica, y pueden usarse como puntos de comparaci\u00F3n para evaluar alineamientos generados por m\u00E9todos bioinform\u00E1ticos basados exclusivamente en secuencias.\u200B El resultado de un alineamiento estructural es una superposici\u00F3n de los conjuntos de coordenadas at\u00F3micas, as\u00ED como una distancia media cuadr\u00E1tica m\u00EDnima (o RMSD, de Root Mean Square Deviation, o ) entre las estructuras b\u00E1sicas de las prote\u00EDnas superpuestas. La RMSD de estructuras alineadas indica las divergencias entre ellas. El alineamiento estructural puede complicarse por la existencia de m\u00FAltiples dominios proteicos en el interior de una o m\u00E1s de las estructuras de entrada, ya que cambios en la orientaci\u00F3n relativa de los dominios entre dos estructuras a alinear pueden exagerar la RMSD artificialmente."@es . . . . . . . . . . "Un alineamiento estructural es un tipo de alineamiento de secuencias basado en la comparaci\u00F3n de la forma. Estos alineamientos intentan establecer equivalencias entre dos o m\u00E1s estructuras de pol\u00EDmeros bas\u00E1ndose en su forma y conformaci\u00F3n tridimensional. El proceso se aplica normalmente a las estructuras terciarias de las prote\u00EDnas, pero tambi\u00E9n puede usarse para largas mol\u00E9culas de ARN. En contraste a la simple superposici\u00F3n estructural, donde al menos se conocen algunos residuos equivalentes de las dos estructuras, el alineamiento estructural no requiere un conocimiento previo de posiciones equivalentes. Es una valiosa herramienta para la comparaci\u00F3n de prote\u00EDnas con baja similitud entre sus secuencias, en donde las relaciones evolutivas entre prote\u00EDnas no pueden ser f\u00E1cilmente detectada"@es . . . . . . . . . . . . . . . . . . . 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\u0627\u0644\u062A\u0634\u0643\u064A\u0644\u064A\u0629 \u0645\u0639\u0631\u0648\u0641\u0629. \u0627\u0644\u062A\u0634\u0643\u064A\u0644\u0627\u062A \u062B\u0644\u0627\u062B\u064A\u0629 \u0627\u0644\u0623\u0628\u0639\u0627\u062F \u0647\u0630\u0647 \u062A\u0639\u0631\u0641 \u0639\u0646 \u0637\u0631\u064A\u0642 \u062F\u0631\u0627\u0633\u0629 \u0627\u0644\u0628\u0644\u0648\u0631\u0627\u062A \u0628\u0627\u0644\u0623\u0634\u0639\u0629 \u0627\u0644\u0633\u064A\u0646\u064A\u0629 \u0623\u0648 NMR spectroscopy. \u0645\u0646 \u0627\u0644\u0645\u0645\u0643\u0646 \u063A\u0646\u062C\u0627\u0632 \u0627\u0644\u062A\u0631\u0627\u0635\u0641 \u0627\u0644\u0628\u0646\u064A\u0648\u064A \u0639\u0644\u0649 \u0628\u0646\u0649 \u064A\u062A\u0645 \u0625\u0646\u062A\u0627\u062C\u0647\u0627 \u0639\u0646 \u0637\u0631\u064A\u0642 \u0637\u0631\u0642 \u0627\u0644\u062A\u0646\u0628\u0624 \u0627\u0644\u0628\u0646\u064A\u0648\u064A. \u0648\u0628\u0627\u0644\u0641\u0639\u0644 \u062A\u0637\u0648\u064A\u0631 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RMSD \u0644\u0628\u064A\u062A\u064A\u0646 \u0645\u062A\u0631\u0627\u0635\u0641\u062A\u064A\u0646 \u064A\u062F\u0644 \u0639\u0644\u0649 \u0645\u062F\u0649 \u0627\u0644\u062A\u0642\u0627\u0631\u0628 \u0648\u0627\u0644\u0634\u0628\u0647 \u0628\u064A\u0646\u0647\u0645\u0627. \u0627\u0644\u062A\u0631\u0627\u0635\u0641 \u0627\u0644\u0628\u0646\u064A\u0648\u064A \u064A\u0645\u0643\u0646 \u0623\u0646 \u064A\u062A\u0639\u0642\u062F \u0628\u0648\u062C\u0648\u062F protein domain \u0645\u062A\u0639\u062F\u062F\u0629 \u0636\u0645\u0646 \u0648\u0627\u062D\u062F \u0623\u0648 \u0623\u0643\u062B\u0631 \u0645\u0646 \u0627\u0644\u0628\u0646\u0649 \u0627\u0644\u0645\u062F\u062E\u0644\u0629\u060C \u0644\u0623\u0646 \u0627\u0644\u062A\u063A\u064A\u0631\u0627\u062A \u0641\u064A \u0627\u0644\u062A\u0648\u062C\u0647\u0627\u062A \u0627\u0644\u0646\u0633\u0628\u064A\u0629 \u0644\u0644\u0646\u0637\u0627\u0642\u0627\u062A \u0628\u064A\u0646 \u0627\u0644\u0628\u0646\u064A\u062A\u064A\u0646 \u0644\u064A\u062D\u062F\u062B \u0627\u0644\u062A\u0631\u0627\u0635\u0641 \u064A\u0645\u0643\u0646 \u0623\u0646 \u064A\u0636\u062E\u0645 \u0643\u062B\u064A\u0631\u0627 \u0627\u0644 \u0622\u0631.\u0625\u0645.\u0625\u0633.\u062F\u064A (\u0627\u0646\u062D\u0631\u0627\u0641 \u0645\u0631\u0628\u0639 \u0627\u0644\u0645\u062A\u0648\u0633\u0637 \u0627\u0644\u062C\u0630\u0631\u064A)."@ar . . . . . "Alineamiento estructural"@es . . . "Strukturn\u00ED alignment je zp\u016Fsob porovn\u00E1v\u00E1n\u00ED polymern\u00EDch struktur na z\u00E1klad\u011B jejich tvaru a prostorov\u00E9ho rozlo\u017Een\u00ED. Krom\u011B ur\u010Dov\u00E1n\u00ED podobnost\u00ED protein\u016F nach\u00E1z\u00ED vyu\u017Eit\u00ED i p\u0159i porovn\u00E1v\u00E1n\u00ED molekul RNA. Ur\u010Den\u00ED podobnosti protein\u016F pat\u0159\u00ED mezi d\u016Fle\u017Eit\u00E9 faktory spr\u00E1vn\u00E9 klasifikace protein\u016F, ze strukturn\u00ED podobnosti s ostatn\u00EDmi proteiny lze vyvodit informace o evolu\u010Dn\u00EDm v\u00FDvoji, nebo biologick\u00E9 funkci, \u010Deho\u017E se vyu\u017E\u00EDv\u00E1 nap\u0159. p\u0159i klasifikaci nov\u011B objeven\u00FDch protein\u016F, u kter\u00FDch je zn\u00E1ma pouze struktura. Pro strukturn\u00ED alignment nen\u00ED pot\u0159eba p\u0159edem zn\u00E1t informace o spole\u010Dn\u00FDch oblastech protein\u016F. V p\u0159\u00EDpad\u011B, \u017Ee maj\u00ED proteiny velkou sekven\u010Dn\u00ED podobnost, vyu\u017E\u00EDv\u00E1 se sp\u00ED\u0161e sekven\u010Dn\u00ED alignment nam\u00EDsto strukturn\u00EDho. Pro tvorbu alignmentu existuj\u00ED des\u00EDtky algoritm\u016F, li\u0161\u00ED se p\u0159edev\u0161\u00EDm v reprezentaci terci\u00E1rn\u00ED struktury a rozd\u00EDln\u00E9mu p\u0159\u00EDstupu ke kvantifikaci rozd\u00EDl\u016F ve struktu\u0159e. Optim\u00E1ln\u00EDm alignmentem naz\u00FDv\u00E1me soustavy sou\u0159adnic v prostoru reprezentuj\u00EDc\u00ED porovn\u00E1van\u00E9 proteiny, kter\u00E9 se p\u0159ekr\u00FDvaj\u00ED tak, aby mezi nimi byla nejmen\u0161\u00ED mo\u017En\u00E1 odchylka."@cs . . . "Um alinhamento estrutural \u00E9 um tipo de alinhamento de sequ\u00EAncias baseado na compara\u00E7\u00E3o da forma das mol\u00E9culas. Estes alinhamentos tentam estabelecer equival\u00EAncias entre duas ou mais estruturas de pol\u00EDmeros baseando-se na sua forma e . O processo normalmente aplica-se \u00E0s das prote\u00EDnas, mas tamb\u00E9m pode ser usado para longas mol\u00E9culas de RNA. Ao contr\u00E1rio da sobreposi\u00E7\u00E3o estrutural simples, onde se conhecem alguns res\u00EDduos equivalentes das duas estruturas, o alinhamento estrutural n\u00E3o requer um conhecimento pr\u00E9vio de posi\u00E7\u00F5es equivalentes. \u00C9 uma valiosa ferramenta para a compara\u00E7\u00E3o de prote\u00EDnas que t\u00EAm poucas semelhan\u00E7as entre as suas sequ\u00EAncias, onde as rela\u00E7\u00F5es evolutivas entre prote\u00EDnas n\u00E3o podem ser facilmente detectadas por t\u00E9cnicas padr\u00E3o de alinhamento de seq\u00FC\u00EAncias. Portanto, o alinh"@pt . . "\u041F\u0440\u043E\u0441\u0442\u0440\u0430\u043D\u0441\u0442\u0432\u0435\u043D\u043D\u043E\u0435 \u0432\u044B\u0440\u0430\u0432\u043D\u0438\u0432\u0430\u043D\u0438\u0435"@ru . . . . . . . . . . . . . . "1107031349"^^ . . "Structural alignment attempts to establish homology between two or more polymer structures based on their shape and three-dimensional conformation. This process is usually applied to protein tertiary structures but can also be used for large RNA molecules. In contrast to simple structural superposition, where at least some equivalent residues of the two structures are known, structural alignment requires no a priori knowledge of equivalent positions. Structural alignment is a valuable tool for the comparison of proteins with low sequence similarity, where evolutionary relationships between proteins cannot be easily detected by standard sequence alignment techniques. Structural alignment can therefore be used to imply evolutionary relationships between proteins that share very little common"@en . . . "Alinhamento estrutural"@pt . . . . "44465"^^ . . . . . "Structural alignment attempts to establish homology between two or more polymer structures based on their shape and three-dimensional conformation. This process is usually applied to protein tertiary structures but can also be used for large RNA molecules. In contrast to simple structural superposition, where at least some equivalent residues of the two structures are known, structural alignment requires no a priori knowledge of equivalent positions. Structural alignment is a valuable tool for the comparison of proteins with low sequence similarity, where evolutionary relationships between proteins cannot be easily detected by standard sequence alignment techniques. Structural alignment can therefore be used to imply evolutionary relationships between proteins that share very little common sequence. However, caution should be used in using the results as evidence for shared evolutionary ancestry because of the possible confounding effects of convergent evolution by which multiple unrelated amino acid sequences converge on a common tertiary structure. Structural alignments can compare two sequences or multiple sequences. Because these alignments rely on information about all the query sequences' three-dimensional conformations, the method can only be used on sequences where these structures are known. These are usually found by X-ray crystallography or NMR spectroscopy. It is possible to perform a structural alignment on structures produced by structure prediction methods. Indeed, evaluating such predictions often requires a structural alignment between the model and the true known structure to assess the model's quality. Structural alignments are especially useful in analyzing data from structural genomics and proteomics efforts, and they can be used as comparison points to evaluate alignments produced by purely sequence-based bioinformatics methods. The outputs of a structural alignment are a superposition of the atomic coordinate sets and a minimal root mean square deviation (RMSD) between the structures. The RMSD of two aligned structures indicates their divergence from one another. Structural alignment can be complicated by the existence of multiple protein domains within one or more of the input structures, because changes in relative orientation of the domains between two structures to be aligned can artificially inflate the RMSD."@en . . 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