Preliminary results of human PrPC protein studied by spectroscopic techniques
• First attempt of XAS study of lyophilized PrPC-Cu(II) complex was successfully made. • Complementary, AFM has shown that PrPC main domain has around 5nm in diameter. • A protocol of fixing PrPC sample on solid substrate was developed for further study. • By using ab-initio calculations, structures...
Ausführliche Beschreibung
Autor*in: |
Nowakowski, Michał [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2017 |
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Schlagwörter: |
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Umfang: |
8 |
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Übergeordnetes Werk: |
Enthalten in: Editorial Comment - Unwala, Darius J. ELSEVIER, 2013, a journal on accelerators, instrumentation and techniques applied to research in nuclear and atomic physics, materials science and related fields in physics, Amsterdam [u.a.] |
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Übergeordnetes Werk: |
volume:411 ; year:2017 ; day:15 ; month:11 ; pages:121-128 ; extent:8 |
Links: |
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DOI / URN: |
10.1016/j.nimb.2017.06.022 |
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10.1016/j.nimb.2017.06.022 doi GBV00000000000021.pica (DE-627)ELV040856305 (ELSEVIER)S0168-583X(17)30696-1 DE-627 ger DE-627 rakwb eng 530 530 DE-600 610 VZ 610 VZ 44.85 bkl Nowakowski, Michał verfasserin aut Preliminary results of human PrPC protein studied by spectroscopic techniques 2017 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • First attempt of XAS study of lyophilized PrPC-Cu(II) complex was successfully made. • Complementary, AFM has shown that PrPC main domain has around 5nm in diameter. • A protocol of fixing PrPC sample on solid substrate was developed for further study. • By using ab-initio calculations, structures of PrPC-Cu(II) binding site were proposed. • The LCF has shown two coexisting Cu(II) binding modes in sample: 4N and 3N+2O. Human prion protein Elsevier AFM Elsevier Neurodegeneration diseases Elsevier Copper binding Elsevier XAS Elsevier Czapla-Masztafiak, Joanna oth Kozak, Maciej oth Zhukov, Igor oth Zhukova, Lilia oth Szlachetko, Jakub oth Kwiatek, Wojciech M. oth Enthalten in Elsevier Unwala, Darius J. ELSEVIER Editorial Comment 2013 a journal on accelerators, instrumentation and techniques applied to research in nuclear and atomic physics, materials science and related fields in physics Amsterdam [u.a.] (DE-627)ELV011304669 volume:411 year:2017 day:15 month:11 pages:121-128 extent:8 https://doi.org/10.1016/j.nimb.2017.06.022 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_40 GBV_ILN_62 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 44.85 Kardiologie Angiologie VZ AR 411 2017 15 1115 121-128 8 045F 530 |
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10.1016/j.nimb.2017.06.022 doi GBV00000000000021.pica (DE-627)ELV040856305 (ELSEVIER)S0168-583X(17)30696-1 DE-627 ger DE-627 rakwb eng 530 530 DE-600 610 VZ 610 VZ 44.85 bkl Nowakowski, Michał verfasserin aut Preliminary results of human PrPC protein studied by spectroscopic techniques 2017 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • First attempt of XAS study of lyophilized PrPC-Cu(II) complex was successfully made. • Complementary, AFM has shown that PrPC main domain has around 5nm in diameter. • A protocol of fixing PrPC sample on solid substrate was developed for further study. • By using ab-initio calculations, structures of PrPC-Cu(II) binding site were proposed. • The LCF has shown two coexisting Cu(II) binding modes in sample: 4N and 3N+2O. Human prion protein Elsevier AFM Elsevier Neurodegeneration diseases Elsevier Copper binding Elsevier XAS Elsevier Czapla-Masztafiak, Joanna oth Kozak, Maciej oth Zhukov, Igor oth Zhukova, Lilia oth Szlachetko, Jakub oth Kwiatek, Wojciech M. oth Enthalten in Elsevier Unwala, Darius J. ELSEVIER Editorial Comment 2013 a journal on accelerators, instrumentation and techniques applied to research in nuclear and atomic physics, materials science and related fields in physics Amsterdam [u.a.] (DE-627)ELV011304669 volume:411 year:2017 day:15 month:11 pages:121-128 extent:8 https://doi.org/10.1016/j.nimb.2017.06.022 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_40 GBV_ILN_62 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 44.85 Kardiologie Angiologie VZ AR 411 2017 15 1115 121-128 8 045F 530 |
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10.1016/j.nimb.2017.06.022 doi GBV00000000000021.pica (DE-627)ELV040856305 (ELSEVIER)S0168-583X(17)30696-1 DE-627 ger DE-627 rakwb eng 530 530 DE-600 610 VZ 610 VZ 44.85 bkl Nowakowski, Michał verfasserin aut Preliminary results of human PrPC protein studied by spectroscopic techniques 2017 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • First attempt of XAS study of lyophilized PrPC-Cu(II) complex was successfully made. • Complementary, AFM has shown that PrPC main domain has around 5nm in diameter. • A protocol of fixing PrPC sample on solid substrate was developed for further study. • By using ab-initio calculations, structures of PrPC-Cu(II) binding site were proposed. • The LCF has shown two coexisting Cu(II) binding modes in sample: 4N and 3N+2O. Human prion protein Elsevier AFM Elsevier Neurodegeneration diseases Elsevier Copper binding Elsevier XAS Elsevier Czapla-Masztafiak, Joanna oth Kozak, Maciej oth Zhukov, Igor oth Zhukova, Lilia oth Szlachetko, Jakub oth Kwiatek, Wojciech M. oth Enthalten in Elsevier Unwala, Darius J. ELSEVIER Editorial Comment 2013 a journal on accelerators, instrumentation and techniques applied to research in nuclear and atomic physics, materials science and related fields in physics Amsterdam [u.a.] (DE-627)ELV011304669 volume:411 year:2017 day:15 month:11 pages:121-128 extent:8 https://doi.org/10.1016/j.nimb.2017.06.022 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_40 GBV_ILN_62 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 44.85 Kardiologie Angiologie VZ AR 411 2017 15 1115 121-128 8 045F 530 |
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10.1016/j.nimb.2017.06.022 doi GBV00000000000021.pica (DE-627)ELV040856305 (ELSEVIER)S0168-583X(17)30696-1 DE-627 ger DE-627 rakwb eng 530 530 DE-600 610 VZ 610 VZ 44.85 bkl Nowakowski, Michał verfasserin aut Preliminary results of human PrPC protein studied by spectroscopic techniques 2017 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • First attempt of XAS study of lyophilized PrPC-Cu(II) complex was successfully made. • Complementary, AFM has shown that PrPC main domain has around 5nm in diameter. • A protocol of fixing PrPC sample on solid substrate was developed for further study. • By using ab-initio calculations, structures of PrPC-Cu(II) binding site were proposed. • The LCF has shown two coexisting Cu(II) binding modes in sample: 4N and 3N+2O. Human prion protein Elsevier AFM Elsevier Neurodegeneration diseases Elsevier Copper binding Elsevier XAS Elsevier Czapla-Masztafiak, Joanna oth Kozak, Maciej oth Zhukov, Igor oth Zhukova, Lilia oth Szlachetko, Jakub oth Kwiatek, Wojciech M. oth Enthalten in Elsevier Unwala, Darius J. ELSEVIER Editorial Comment 2013 a journal on accelerators, instrumentation and techniques applied to research in nuclear and atomic physics, materials science and related fields in physics Amsterdam [u.a.] (DE-627)ELV011304669 volume:411 year:2017 day:15 month:11 pages:121-128 extent:8 https://doi.org/10.1016/j.nimb.2017.06.022 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_40 GBV_ILN_62 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 44.85 Kardiologie Angiologie VZ AR 411 2017 15 1115 121-128 8 045F 530 |
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10.1016/j.nimb.2017.06.022 doi GBV00000000000021.pica (DE-627)ELV040856305 (ELSEVIER)S0168-583X(17)30696-1 DE-627 ger DE-627 rakwb eng 530 530 DE-600 610 VZ 610 VZ 44.85 bkl Nowakowski, Michał verfasserin aut Preliminary results of human PrPC protein studied by spectroscopic techniques 2017 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • First attempt of XAS study of lyophilized PrPC-Cu(II) complex was successfully made. • Complementary, AFM has shown that PrPC main domain has around 5nm in diameter. • A protocol of fixing PrPC sample on solid substrate was developed for further study. • By using ab-initio calculations, structures of PrPC-Cu(II) binding site were proposed. • The LCF has shown two coexisting Cu(II) binding modes in sample: 4N and 3N+2O. Human prion protein Elsevier AFM Elsevier Neurodegeneration diseases Elsevier Copper binding Elsevier XAS Elsevier Czapla-Masztafiak, Joanna oth Kozak, Maciej oth Zhukov, Igor oth Zhukova, Lilia oth Szlachetko, Jakub oth Kwiatek, Wojciech M. oth Enthalten in Elsevier Unwala, Darius J. ELSEVIER Editorial Comment 2013 a journal on accelerators, instrumentation and techniques applied to research in nuclear and atomic physics, materials science and related fields in physics Amsterdam [u.a.] (DE-627)ELV011304669 volume:411 year:2017 day:15 month:11 pages:121-128 extent:8 https://doi.org/10.1016/j.nimb.2017.06.022 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_21 GBV_ILN_22 GBV_ILN_24 GBV_ILN_40 GBV_ILN_62 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 44.85 Kardiologie Angiologie VZ AR 411 2017 15 1115 121-128 8 045F 530 |
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Nowakowski, Michał |
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Nowakowski, Michał |
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title_sort |
preliminary results of human prpc protein studied by spectroscopic techniques |
title_auth |
Preliminary results of human PrPC protein studied by spectroscopic techniques |
abstract |
• First attempt of XAS study of lyophilized PrPC-Cu(II) complex was successfully made. • Complementary, AFM has shown that PrPC main domain has around 5nm in diameter. • A protocol of fixing PrPC sample on solid substrate was developed for further study. • By using ab-initio calculations, structures of PrPC-Cu(II) binding site were proposed. • The LCF has shown two coexisting Cu(II) binding modes in sample: 4N and 3N+2O. |
abstractGer |
• First attempt of XAS study of lyophilized PrPC-Cu(II) complex was successfully made. • Complementary, AFM has shown that PrPC main domain has around 5nm in diameter. • A protocol of fixing PrPC sample on solid substrate was developed for further study. • By using ab-initio calculations, structures of PrPC-Cu(II) binding site were proposed. • The LCF has shown two coexisting Cu(II) binding modes in sample: 4N and 3N+2O. |
abstract_unstemmed |
• First attempt of XAS study of lyophilized PrPC-Cu(II) complex was successfully made. • Complementary, AFM has shown that PrPC main domain has around 5nm in diameter. • A protocol of fixing PrPC sample on solid substrate was developed for further study. • By using ab-initio calculations, structures of PrPC-Cu(II) binding site were proposed. • The LCF has shown two coexisting Cu(II) binding modes in sample: 4N and 3N+2O. |
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title_short |
Preliminary results of human PrPC protein studied by spectroscopic techniques |
url |
https://doi.org/10.1016/j.nimb.2017.06.022 |
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Czapla-Masztafiak, Joanna Kozak, Maciej Zhukov, Igor Zhukova, Lilia Szlachetko, Jakub Kwiatek, Wojciech M. |
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Czapla-Masztafiak, Joanna Kozak, Maciej Zhukov, Igor Zhukova, Lilia Szlachetko, Jakub Kwiatek, Wojciech M. |
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