Performance of phased rotation, conformation and translation function: accurate protein model building with tripeptidic and terapeptidic fragments

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62157124%3A16370%2F10%3A00002651" target="_blank" >RIV/62157124:16370/10:00002651 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Performance of phased rotation, conformation and translation function: accurate protein model building with tripeptidic and terapeptidic fragments

Popis výsledku v původním jazyce

The automatic building of protein structures with tripeptidic and tetrapeptidic fragments was investigated. The oligopeptidic conformers were positioned in the electron-density map by a phased rotation, conformation and translation function and refined by a real-space refinement. The number of successfully located fragments lies within the interval 75 ? 95 % depending on the resolution and phase quality. The overlaps of partially located fragments were analyzed. The correctly positioned fragments were connected into chains. Chains formed in this way are extended directly into the electron density and a sequence was assigned. In the initial stage of the model building the number of located fragments was between 60 ? 95 % but this number could be increased by several cycles of reciprocal-space refinement and automatic model re-building. A nearly complete structure can be obtained on the condition that the resolution is reasonable. Computer graphics will only needed for a final check and

Název v anglickém jazyce

Performance of phased rotation, conformation and translation function: accurate protein model building with tripeptidic and terapeptidic fragments

Popis výsledku anglicky

The automatic building of protein structures with tripeptidic and tetrapeptidic fragments was investigated. The oligopeptidic conformers were positioned in the electron-density map by a phased rotation, conformation and translation function and refined by a real-space refinement. The number of successfully located fragments lies within the interval 75 ? 95 % depending on the resolution and phase quality. The overlaps of partially located fragments were analyzed. The correctly positioned fragments were connected into chains. Chains formed in this way are extended directly into the electron density and a sequence was assigned. In the initial stage of the model building the number of located fragments was between 60 ? 95 % but this number could be increased by several cycles of reciprocal-space refinement and automatic model re-building. A nearly complete structure can be obtained on the condition that the resolution is reasonable. Computer graphics will only needed for a final check and

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

FR - Farmakologie a lékárnická chemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2010

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Crystallographica Section D

ISSN

0907-4449

e-ISSN

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Svazek periodika

66

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

12

Strana od-do

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Kód UT WoS článku

000281635500007

EID výsledku v databázi Scopus

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