The core of apomyoglobin E-form folds at the diffusion limit
[Auszug] How does the collapse of a protein proceed from an extended, disordered structure to a compact structure? What drives the process and at what rate? We have explored this vital issue with a form of apomyoglobin that is highly disordered — apoMb, myoglobin with the heme group extracted ...
Gespeichert in:
| Autor*in: |
Gilmanshin, Rudolf [verfasserIn] Callender, Robert H. [verfasserIn] Dyer, R. Brian [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
s.l.: Nature Publishing Group ; 1998 |
|---|
| Umfang: |
3 |
|---|
| Reproduktion: |
Nature Archives 1869 - 2009 |
|---|---|
| Übergeordnetes Werk: |
In: Nature structural biology - New York, NY : Nature America, 1994, 5(1998), 5, Seite 363-365 |
| Übergeordnetes Werk: |
volume:5 ; year:1998 ; number:5 ; month:00 ; pages:363-365 ; extent:3 |
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| DOI / URN: |
10.1038/nsb0598-363 |
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10.1038/nsb0598-363 doi (DE-627)NLEJ231626177 DE-627 ger DE-627 rakwb eng XD-US Gilmanshin, Rudolf verfasserin aut The core of apomyoglobin E-form folds at the diffusion limit [s.l.] Nature Publishing Group 1998 3 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier [Auszug] How does the collapse of a protein proceed from an extended, disordered structure to a compact structure? What drives the process and at what rate? We have explored this vital issue with a form of apomyoglobin that is highly disordered — apoMb, myoglobin with the heme group extracted ... Nature Archives 1869 - 2009 Callender, Robert H. verfasserin aut Dyer, R. Brian verfasserin aut In Nature structural biology New York, NY : Nature America, 1994 5(1998), 5, Seite 363-365 (DE-627)NLEJ227682378 (DE-600)1494960-x nnns volume:5 year:1998 number:5 month:00 pages:363-365 extent:3 http://dx.doi.org/10.1038/nsb0598-363 application/pdf Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-NTA GBV_NL_ARTICLE AR 5 1998 5 0 363-365 3 |
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10.1038/nsb0598-363 doi (DE-627)NLEJ231626177 DE-627 ger DE-627 rakwb eng XD-US Gilmanshin, Rudolf verfasserin aut The core of apomyoglobin E-form folds at the diffusion limit [s.l.] Nature Publishing Group 1998 3 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier [Auszug] How does the collapse of a protein proceed from an extended, disordered structure to a compact structure? What drives the process and at what rate? We have explored this vital issue with a form of apomyoglobin that is highly disordered — apoMb, myoglobin with the heme group extracted ... Nature Archives 1869 - 2009 Callender, Robert H. verfasserin aut Dyer, R. Brian verfasserin aut In Nature structural biology New York, NY : Nature America, 1994 5(1998), 5, Seite 363-365 (DE-627)NLEJ227682378 (DE-600)1494960-x nnns volume:5 year:1998 number:5 month:00 pages:363-365 extent:3 http://dx.doi.org/10.1038/nsb0598-363 application/pdf Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-NTA GBV_NL_ARTICLE AR 5 1998 5 0 363-365 3 |
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10.1038/nsb0598-363 doi (DE-627)NLEJ231626177 DE-627 ger DE-627 rakwb eng XD-US Gilmanshin, Rudolf verfasserin aut The core of apomyoglobin E-form folds at the diffusion limit [s.l.] Nature Publishing Group 1998 3 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier [Auszug] How does the collapse of a protein proceed from an extended, disordered structure to a compact structure? What drives the process and at what rate? We have explored this vital issue with a form of apomyoglobin that is highly disordered — apoMb, myoglobin with the heme group extracted ... Nature Archives 1869 - 2009 Callender, Robert H. verfasserin aut Dyer, R. Brian verfasserin aut In Nature structural biology New York, NY : Nature America, 1994 5(1998), 5, Seite 363-365 (DE-627)NLEJ227682378 (DE-600)1494960-x nnns volume:5 year:1998 number:5 month:00 pages:363-365 extent:3 http://dx.doi.org/10.1038/nsb0598-363 application/pdf Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-NTA GBV_NL_ARTICLE AR 5 1998 5 0 363-365 3 |
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10.1038/nsb0598-363 doi (DE-627)NLEJ231626177 DE-627 ger DE-627 rakwb eng XD-US Gilmanshin, Rudolf verfasserin aut The core of apomyoglobin E-form folds at the diffusion limit [s.l.] Nature Publishing Group 1998 3 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier [Auszug] How does the collapse of a protein proceed from an extended, disordered structure to a compact structure? What drives the process and at what rate? We have explored this vital issue with a form of apomyoglobin that is highly disordered — apoMb, myoglobin with the heme group extracted ... Nature Archives 1869 - 2009 Callender, Robert H. verfasserin aut Dyer, R. Brian verfasserin aut In Nature structural biology New York, NY : Nature America, 1994 5(1998), 5, Seite 363-365 (DE-627)NLEJ227682378 (DE-600)1494960-x nnns volume:5 year:1998 number:5 month:00 pages:363-365 extent:3 http://dx.doi.org/10.1038/nsb0598-363 application/pdf Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-NTA GBV_NL_ARTICLE AR 5 1998 5 0 363-365 3 |
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10.1038/nsb0598-363 doi (DE-627)NLEJ231626177 DE-627 ger DE-627 rakwb eng XD-US Gilmanshin, Rudolf verfasserin aut The core of apomyoglobin E-form folds at the diffusion limit [s.l.] Nature Publishing Group 1998 3 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier [Auszug] How does the collapse of a protein proceed from an extended, disordered structure to a compact structure? What drives the process and at what rate? We have explored this vital issue with a form of apomyoglobin that is highly disordered — apoMb, myoglobin with the heme group extracted ... Nature Archives 1869 - 2009 Callender, Robert H. verfasserin aut Dyer, R. Brian verfasserin aut In Nature structural biology New York, NY : Nature America, 1994 5(1998), 5, Seite 363-365 (DE-627)NLEJ227682378 (DE-600)1494960-x nnns volume:5 year:1998 number:5 month:00 pages:363-365 extent:3 http://dx.doi.org/10.1038/nsb0598-363 application/pdf Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-NTA GBV_NL_ARTICLE AR 5 1998 5 0 363-365 3 |
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[Auszug] How does the collapse of a protein proceed from an extended, disordered structure to a compact structure? What drives the process and at what rate? We have explored this vital issue with a form of apomyoglobin that is highly disordered — apoMb, myoglobin with the heme group extracted ... |
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