Sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy

Significance of intrinsic disorder in biological systems, nuclear magnetism and different methods for its use in protein structure determination have been reviewed. These methods include the use of different detection schemes for nuclear magnetic resonance spectroscopy, observables and their relatio...

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Main Author: Salovaara, Santeri
Other Authors: Matemaattis-luonnontieteellinen tiedekunta, Faculty of Sciences, Kemian laitos, Department of Chemistry, Jyväskylän yliopisto, University of Jyväskylä
Format: Master's thesis
Language:eng
Published: 2018
Subjects:
Online Access: https://jyx.jyu.fi/handle/123456789/58788
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author Salovaara, Santeri
author2 Matemaattis-luonnontieteellinen tiedekunta Faculty of Sciences Kemian laitos Department of Chemistry Jyväskylän yliopisto University of Jyväskylä
author_facet Salovaara, Santeri Matemaattis-luonnontieteellinen tiedekunta Faculty of Sciences Kemian laitos Department of Chemistry Jyväskylän yliopisto University of Jyväskylä Salovaara, Santeri Matemaattis-luonnontieteellinen tiedekunta Faculty of Sciences Kemian laitos Department of Chemistry Jyväskylän yliopisto University of Jyväskylä
author_sort Salovaara, Santeri
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description Significance of intrinsic disorder in biological systems, nuclear magnetism and different methods for its use in protein structure determination have been reviewed. These methods include the use of different detection schemes for nuclear magnetic resonance spectroscopy, observables and their relation to structure, computational methods and sequential assignment procedure. In addition an intrinsically disordered protein, bacterial interleukin receptor 1, related to pathological pathways of periodontitis is covered in in detail. Sequential backbone chemical shift assignment and structural propensity estimation calculations based on chemical shifts of bacterial interleukin receptor 1 have been carried out. Secondary structure estimation confirms that bacterial interleukin receptor 1 is an intrinsically disordered protein with some transient alpha-helicity in the middle of its primary structure.
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spellingShingle Salovaara, Santeri Sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy intrinsic disorder Fysikaalinen kemia Physical Chemistry 4032 NMR-spektroskopia spektroskopia proteiinit NMR spectroscopy spectroscopy proteins
title Sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy
title_full Sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy
title_fullStr Sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy Sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy
title_full_unstemmed Sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy Sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy
title_short Sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy
title_sort sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy
title_txtP Sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy
topic intrinsic disorder Fysikaalinen kemia Physical Chemistry 4032 NMR-spektroskopia spektroskopia proteiinit NMR spectroscopy spectroscopy proteins
topic_facet 4032 Fysikaalinen kemia NMR spectroscopy NMR-spektroskopia Physical Chemistry intrinsic disorder proteiinit proteins spectroscopy spektroskopia
url https://jyx.jyu.fi/handle/123456789/58788 http://www.urn.fi/URN:NBN:fi:jyu-201806293414
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