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...

Full description

Bibliographic Details
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/123456789/58766
_version_ 1826225694463492096
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
datasource_str_mv jyx
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.
first_indexed 2019-08-19T08:21:17Z
format Pro gradu
free_online_boolean 1
fullrecord [{"key": "dc.contributor.advisor", "value": "Permi, Perttu", "language": "", "element": "contributor", "qualifier": "advisor", "schema": "dc"}, {"key": "dc.contributor.advisor", "value": "Aitio, Helena", "language": "", "element": "contributor", "qualifier": "advisor", "schema": "dc"}, {"key": "dc.contributor.author", "value": "Salovaara, Santeri", "language": "", "element": "contributor", "qualifier": "author", "schema": "dc"}, {"key": "dc.date.accessioned", "value": "2018-06-28T11:10:35Z", "language": null, "element": "date", "qualifier": "accessioned", "schema": "dc"}, {"key": "dc.date.available", "value": "2018-06-28T11:10:35Z", "language": null, "element": "date", "qualifier": "available", "schema": "dc"}, {"key": "dc.date.issued", "value": "2018", "language": "", "element": "date", "qualifier": "issued", "schema": "dc"}, {"key": "dc.identifier.uri", "value": "https://jyx.jyu.fi/handle/123456789/58766", "language": null, "element": "identifier", "qualifier": "uri", "schema": "dc"}, {"key": "dc.description.abstract", "value": "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.", "language": "en", "element": "description", "qualifier": "abstract", "schema": "dc"}, {"key": "dc.description.provenance", "value": "Submitted by Riitta Pitk\u00e4nen (rpitkane@jyu.fi) on 2018-06-28T11:10:35Z\nNo. of bitstreams: 0", "language": "en", "element": "description", "qualifier": "provenance", "schema": "dc"}, {"key": "dc.description.provenance", "value": "Made available in DSpace on 2018-06-28T11:10:35Z (GMT). No. of bitstreams: 0\n Previous issue date: 2018", "language": "en", "element": "description", "qualifier": "provenance", "schema": "dc"}, {"key": "dc.format.extent", "value": "78", "language": "", "element": "format", "qualifier": "extent", "schema": "dc"}, {"key": "dc.format.mimetype", "value": "application/pdf", "language": null, "element": "format", "qualifier": "mimetype", "schema": "dc"}, {"key": "dc.language.iso", "value": "eng", "language": null, "element": "language", "qualifier": "iso", "schema": "dc"}, {"key": "dc.rights", "value": "In Copyright", "language": "en", "element": "rights", "qualifier": null, "schema": "dc"}, {"key": "dc.subject.other", "value": "Intrinsic disorder", "language": "", "element": "subject", "qualifier": "other", "schema": "dc"}, {"key": "dc.title", "value": "Sequential assignment of the intrinsically disordered protein bacterial interleukin receptor 1 with nuclear magnetic resonance spectroscopy", "language": "", "element": "title", "qualifier": null, "schema": "dc"}, {"key": "dc.type", "value": "master thesis", "language": null, "element": "type", "qualifier": null, "schema": "dc"}, {"key": "dc.identifier.urn", "value": "URN:NBN:fi:jyu-201806283389", "language": "", "element": "identifier", "qualifier": "urn", "schema": "dc"}, {"key": "dc.type.ontasot", "value": "Pro gradu -tutkielma", "language": "fi", "element": "type", "qualifier": "ontasot", "schema": "dc"}, {"key": "dc.type.ontasot", "value": "Master\u2019s thesis", "language": "en", "element": "type", "qualifier": "ontasot", "schema": "dc"}, {"key": "dc.contributor.faculty", "value": "Matemaattis-luonnontieteellinen tiedekunta", "language": "fi", "element": "contributor", "qualifier": "faculty", "schema": "dc"}, {"key": "dc.contributor.faculty", "value": "Faculty of Sciences", "language": "en", "element": "contributor", "qualifier": "faculty", "schema": "dc"}, {"key": "dc.contributor.department", "value": "Kemian laitos", "language": "fi", "element": "contributor", "qualifier": "department", "schema": "dc"}, {"key": "dc.contributor.department", "value": "Department of Chemistry", "language": "en", "element": "contributor", "qualifier": "department", "schema": "dc"}, {"key": "dc.contributor.organization", "value": "Jyv\u00e4skyl\u00e4n yliopisto", "language": "fi", "element": "contributor", "qualifier": "organization", "schema": "dc"}, {"key": "dc.contributor.organization", "value": "University of Jyv\u00e4skyl\u00e4", "language": "en", "element": "contributor", "qualifier": "organization", "schema": "dc"}, {"key": "dc.subject.discipline", "value": "Fysikaalinen kemia", "language": "fi", "element": "subject", "qualifier": "discipline", "schema": "dc"}, {"key": "dc.subject.discipline", "value": "Physical Chemistry", "language": "en", "element": "subject", "qualifier": "discipline", "schema": "dc"}, {"key": "yvv.contractresearch.funding", "value": "0", "language": "", "element": "contractresearch", "qualifier": "funding", "schema": "yvv"}, {"key": "dc.type.coar", "value": "http://purl.org/coar/resource_type/c_bdcc", "language": null, "element": "type", "qualifier": "coar", "schema": "dc"}, {"key": "dc.rights.accesslevel", "value": "openAccess", "language": null, "element": "rights", "qualifier": "accesslevel", "schema": "dc"}, {"key": "dc.type.publication", "value": "masterThesis", "language": null, "element": "type", "qualifier": "publication", "schema": "dc"}, {"key": "dc.subject.oppiainekoodi", "value": "4032", "language": "", "element": "subject", "qualifier": "oppiainekoodi", "schema": "dc"}, {"key": "dc.subject.yso", "value": "NMR-spektroskopia", "language": null, "element": "subject", "qualifier": "yso", "schema": "dc"}, {"key": "dc.subject.yso", "value": "spektroskopia", "language": null, "element": "subject", "qualifier": "yso", "schema": "dc"}, {"key": "dc.subject.yso", "value": "proteiinit", "language": null, "element": "subject", "qualifier": "yso", "schema": "dc"}, {"key": "dc.subject.yso", "value": "resonanssi", "language": null, "element": "subject", "qualifier": "yso", "schema": "dc"}, {"key": "dc.subject.yso", "value": "NMR spectroscopy", "language": null, "element": "subject", "qualifier": "yso", "schema": "dc"}, {"key": "dc.subject.yso", "value": "spectroscopy", "language": null, "element": "subject", "qualifier": "yso", "schema": "dc"}, {"key": "dc.subject.yso", "value": "proteins", "language": null, "element": "subject", "qualifier": "yso", "schema": "dc"}, {"key": "dc.subject.yso", "value": "resonance", "language": null, "element": "subject", "qualifier": "yso", "schema": "dc"}, {"key": "dc.format.content", "value": "fulltext", "language": null, "element": "format", "qualifier": "content", "schema": "dc"}, {"key": "dc.rights.url", "value": "https://rightsstatements.org/page/InC/1.0/", "language": null, "element": "rights", "qualifier": "url", "schema": "dc"}, {"key": "dc.type.okm", "value": "G2", "language": null, "element": "type", "qualifier": "okm", "schema": "dc"}]
id jyx.123456789_58766
language eng
last_indexed 2025-02-18T10:54:39Z
main_date 2018-01-01T00:00:00Z
main_date_str 2018
online_boolean 1
online_urls_str_mv {"url":"https:\/\/jyx.jyu.fi\/bitstreams\/cea19e12-7fc6-4a1a-8d71-732654db8f15\/download","text":"URN:NBN:fi:jyu-201806283389.pdf","source":"jyx","mediaType":"application\/pdf"}
publishDate 2018
record_format qdc
source_str_mv jyx
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 resonanssi NMR spectroscopy spectroscopy proteins resonance
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 resonanssi NMR spectroscopy spectroscopy proteins resonance
topic_facet 4032 Fysikaalinen kemia Intrinsic disorder NMR spectroscopy NMR-spektroskopia Physical Chemistry proteiinit proteins resonance resonanssi spectroscopy spektroskopia
url https://jyx.jyu.fi/handle/123456789/58766 http://www.urn.fi/URN:NBN:fi:jyu-201806283389
work_keys_str_mv AT salovaarasanteri sequentialassignmentoftheintrinsicallydisorderedproteinbacterialinterleukinrece