Does collagen microunfolding stimulate fibril formation?
Abstract The data on the effect of temperature on the kinetics of collagen fibril formation at physiological pH values and ionic strength in the temperature range 26–39°C have been analyzed. The temperature of 35°C optimal for collagen fibril formation has been defined as the point of inflection for...
Ausführliche Beschreibung
Autor*in: |
Nikolaeva, T. I. [verfasserIn] |
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Format: |
Artikel |
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Sprache: |
Englisch |
Erschienen: |
2009 |
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Anmerkung: |
© Pleiades Publishing, Ltd. 2009 |
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Übergeordnetes Werk: |
Enthalten in: Biophysics - SP MAIK Nauka/Interperiodica, 1957, 54(2009), 6 vom: Dez., Seite 683-685 |
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Übergeordnetes Werk: |
volume:54 ; year:2009 ; number:6 ; month:12 ; pages:683-685 |
Links: |
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DOI / URN: |
10.1134/S0006350909060049 |
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Katalog-ID: |
OLC2067720066 |
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10.1134/S0006350909060049 doi (DE-627)OLC2067720066 (DE-He213)S0006350909060049-p DE-627 ger DE-627 rakwb eng 570 530 VZ 12 ssgn BIODIV DE-30 fid Nikolaeva, T. I. verfasserin aut Does collagen microunfolding stimulate fibril formation? 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Pleiades Publishing, Ltd. 2009 Abstract The data on the effect of temperature on the kinetics of collagen fibril formation at physiological pH values and ionic strength in the temperature range 26–39°C have been analyzed. The temperature of 35°C optimal for collagen fibril formation has been defined as the point of inflection for half-maximal turbidity and collagen molecule microunfolding values, which corresponds to the temperature of the first transition on the heat absorption curve. The temperature range (32–35°C) in which collagen microunfolding stimulates fibril formation has been determined. Kuznetsova, S. M. aut Tiktopulo, E. I. aut Enthalten in Biophysics SP MAIK Nauka/Interperiodica, 1957 54(2009), 6 vom: Dez., Seite 683-685 (DE-627)12909191X (DE-600)6617-5 (DE-576)014427281 0006-3509 nnns volume:54 year:2009 number:6 month:12 pages:683-685 https://doi.org/10.1134/S0006350909060049 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2004 GBV_ILN_4012 AR 54 2009 6 12 683-685 |
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10.1134/S0006350909060049 doi (DE-627)OLC2067720066 (DE-He213)S0006350909060049-p DE-627 ger DE-627 rakwb eng 570 530 VZ 12 ssgn BIODIV DE-30 fid Nikolaeva, T. I. verfasserin aut Does collagen microunfolding stimulate fibril formation? 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Pleiades Publishing, Ltd. 2009 Abstract The data on the effect of temperature on the kinetics of collagen fibril formation at physiological pH values and ionic strength in the temperature range 26–39°C have been analyzed. The temperature of 35°C optimal for collagen fibril formation has been defined as the point of inflection for half-maximal turbidity and collagen molecule microunfolding values, which corresponds to the temperature of the first transition on the heat absorption curve. The temperature range (32–35°C) in which collagen microunfolding stimulates fibril formation has been determined. Kuznetsova, S. M. aut Tiktopulo, E. I. aut Enthalten in Biophysics SP MAIK Nauka/Interperiodica, 1957 54(2009), 6 vom: Dez., Seite 683-685 (DE-627)12909191X (DE-600)6617-5 (DE-576)014427281 0006-3509 nnns volume:54 year:2009 number:6 month:12 pages:683-685 https://doi.org/10.1134/S0006350909060049 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2004 GBV_ILN_4012 AR 54 2009 6 12 683-685 |
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10.1134/S0006350909060049 doi (DE-627)OLC2067720066 (DE-He213)S0006350909060049-p DE-627 ger DE-627 rakwb eng 570 530 VZ 12 ssgn BIODIV DE-30 fid Nikolaeva, T. I. verfasserin aut Does collagen microunfolding stimulate fibril formation? 2009 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Pleiades Publishing, Ltd. 2009 Abstract The data on the effect of temperature on the kinetics of collagen fibril formation at physiological pH values and ionic strength in the temperature range 26–39°C have been analyzed. The temperature of 35°C optimal for collagen fibril formation has been defined as the point of inflection for half-maximal turbidity and collagen molecule microunfolding values, which corresponds to the temperature of the first transition on the heat absorption curve. The temperature range (32–35°C) in which collagen microunfolding stimulates fibril formation has been determined. Kuznetsova, S. M. aut Tiktopulo, E. I. aut Enthalten in Biophysics SP MAIK Nauka/Interperiodica, 1957 54(2009), 6 vom: Dez., Seite 683-685 (DE-627)12909191X (DE-600)6617-5 (DE-576)014427281 0006-3509 nnns volume:54 year:2009 number:6 month:12 pages:683-685 https://doi.org/10.1134/S0006350909060049 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2004 GBV_ILN_4012 AR 54 2009 6 12 683-685 |
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Abstract The data on the effect of temperature on the kinetics of collagen fibril formation at physiological pH values and ionic strength in the temperature range 26–39°C have been analyzed. The temperature of 35°C optimal for collagen fibril formation has been defined as the point of inflection for half-maximal turbidity and collagen molecule microunfolding values, which corresponds to the temperature of the first transition on the heat absorption curve. The temperature range (32–35°C) in which collagen microunfolding stimulates fibril formation has been determined. © Pleiades Publishing, Ltd. 2009 |
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Abstract The data on the effect of temperature on the kinetics of collagen fibril formation at physiological pH values and ionic strength in the temperature range 26–39°C have been analyzed. The temperature of 35°C optimal for collagen fibril formation has been defined as the point of inflection for half-maximal turbidity and collagen molecule microunfolding values, which corresponds to the temperature of the first transition on the heat absorption curve. The temperature range (32–35°C) in which collagen microunfolding stimulates fibril formation has been determined. © Pleiades Publishing, Ltd. 2009 |
abstract_unstemmed |
Abstract The data on the effect of temperature on the kinetics of collagen fibril formation at physiological pH values and ionic strength in the temperature range 26–39°C have been analyzed. The temperature of 35°C optimal for collagen fibril formation has been defined as the point of inflection for half-maximal turbidity and collagen molecule microunfolding values, which corresponds to the temperature of the first transition on the heat absorption curve. The temperature range (32–35°C) in which collagen microunfolding stimulates fibril formation has been determined. © Pleiades Publishing, Ltd. 2009 |
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I.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Does collagen microunfolding stimulate fibril formation?</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2009</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Pleiades Publishing, Ltd. 2009</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract The data on the effect of temperature on the kinetics of collagen fibril formation at physiological pH values and ionic strength in the temperature range 26–39°C have been analyzed. 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