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rdf:type
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Description
| - Ve studii jsou prezentovány MD simulace na celkové škále 450 ns různě velkých fragmentů proteinu p18INK4c. (cs)
- Ankyrin repeat proteins (ARPs) appear to be abundant in organisms from all phyla, and play critical regulatory roles, mediating specific interactions with target biomolecules and thus ordering the sequence of events in diverse cellular processes. ARPs possess a non-globular scaffold consisting of repeating motifs named ankyrin (ANK) repeats, which stack on each other. The modular architecture of ARPs provides a new paradigm for understanding protein stability and folding mechanisms. In the present study, the stability of various C-terminal fragments of the ARP p18(INK4c) was investigated by all-atomic 450 ns molecular dynamics (MD) simulations in explicit water solvent. Only motifs with at least two ANK repeats made stable systems in the available timescale. All smaller fragments were unstable, readily losing their native fold and alpha-helical content. Since each non-terminal ANK repeat has two hydrophobic sides, we may hypothesize that at least one hydrophobic side must be fully covered and shielded
- Ankyrin repeat proteins (ARPs) appear to be abundant in organisms from all phyla, and play critical regulatory roles, mediating specific interactions with target biomolecules and thus ordering the sequence of events in diverse cellular processes. ARPs possess a non-globular scaffold consisting of repeating motifs named ankyrin (ANK) repeats, which stack on each other. The modular architecture of ARPs provides a new paradigm for understanding protein stability and folding mechanisms. In the present study, the stability of various C-terminal fragments of the ARP p18(INK4c) was investigated by all-atomic 450 ns molecular dynamics (MD) simulations in explicit water solvent. Only motifs with at least two ANK repeats made stable systems in the available timescale. All smaller fragments were unstable, readily losing their native fold and alpha-helical content. Since each non-terminal ANK repeat has two hydrophobic sides, we may hypothesize that at least one hydrophobic side must be fully covered and shielded (en)
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Title
| - Two C-terminal ankyrin repeats form the minimal stable unit of the ankyrin repeat protein p18INK4c
- Two C-terminal ankyrin repeats form the minimal stable unit of the ankyrin repeat protein p18INK4c (en)
- Dva C-terminální ankyrinové motivy tvoří minimální stabilní jednotku proteinu p18INK4c (cs)
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skos:prefLabel
| - Two C-terminal ankyrin repeats form the minimal stable unit of the ankyrin repeat protein p18INK4c
- Two C-terminal ankyrin repeats form the minimal stable unit of the ankyrin repeat protein p18INK4c (en)
- Dva C-terminální ankyrinové motivy tvoří minimální stabilní jednotku proteinu p18INK4c (cs)
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skos:notation
| - RIV/61989592:15310/08:00005479!RIV09-MSM-15310___
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
| - P(LC512), Z(MSM6198959216)
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http://linked.open...iv/cisloPeriodika
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/61989592:15310/08:00005479
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - Ankyrin repeat; p18INK4c; Minimal stable unit; Fragmentation; Molecular dynamics (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...odStatuVydavatele
| - DE - Spolková republika Německo
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http://linked.open...ontrolniKodProRIV
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http://linked.open...i/riv/nazevZdroje
| - Journal of Molecular Modeling
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...cetTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...UplatneniVysledku
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http://linked.open...v/svazekPeriodika
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http://linked.open...iv/tvurceVysledku
| - Otyepka, Michal
- Banáš, Pavel
- Sklenovský, Petr
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http://linked.open...n/vavai/riv/zamer
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issn
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number of pages
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http://localhost/t...ganizacniJednotka
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is http://linked.open...avai/riv/vysledek
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