Studies of the collagen fold formation in aqueous solutions of α-gelatin. II

Studies of the collagen fold formation in aqueous solutions of α-gelatin. II

Optical rotation and density studies have been performed as a function of time on solutions of a single‐strand gelatin in salt‐free solutions and in solutions containing sodium bromide, tetramethyl and tetrabutylammonium bromide. The reversion to the collagen fold is shown to be first order in all c...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biopolymers 1980-01, Vol.19 (1), p.147-164
Hauptverfasser: Eagland, D., Pilling, G.
Format: Artikel
Sprache:eng
Schlagworte:
Animals
Collagen
Gelatin
Osmolar Concentration
Protein Conformation
Rats
Tendons
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 164
container_issue 1
container_start_page 147
container_title Biopolymers
container_volume 19
creator Eagland, D.
Pilling, G.
description Optical rotation and density studies have been performed as a function of time on solutions of a single‐strand gelatin in salt‐free solutions and in solutions containing sodium bromide, tetramethyl and tetrabutylammonium bromide. The reversion to the collagen fold is shown to be first order in all cases but undergoes a change in magnitude as a function of an aggregation process which occurs at a concentration of approximately 0.1% w/v. The structuring effects of the electrolytes on the solvent are shown to relate to the extent of helix regeneration by the protein, in the presence of the electrolyte. The extent of helix regeneration is also shown to relate to the thickness of the electric double layer surrounding the protein molecule.
doi_str_mv 10.1002/bip.1980.360190110
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_75096562</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>75096562</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3040-9104c4d4946badcaae26816245b531825e6f80cbf5e6cb5f8baaf254761758ba3</originalsourceid><addsrcrecordid>eNqNkMtOg0AYhSdGU2v1BUxMWLkD_7kCiRtttBLrJbGmy8kAQ0UpVAaifSxfxGdykKZx6WZu__nOnByEjjF4GICcxfnKw2EAHhWAQ8AYdtAQQ-i7QAKyi4YAIFzKCd9HB8a8AjBGMQzQwKc-0JAO0d1T06a5Nk6VOc2LdpKqKNRCl05WFald6qVq8qp08tJR762uWuOYqmi7t1_m-8td6MJqSs-JokO0l6nC6KPNPkLP11ez8Y07fZhE44upm1Bg4IYYWMJSFjIRqzRRShMRYEEYjznFAeFaZAEkcWYPScyzIFYqI5z5AvvcXugInfa-q7qyqUwjl7lJtI1edhGlzyEUXBArJL0wqStjap3JVZ0vVb2WGGTXobQdyq5Due3QQicb9zZe6nSLbEqz8_N-_pEXev0PR3kZPf61d3s8N43-3OKqfpPCfsHl_H4i-f1sfhuOsQzoD8i7jZ4</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>75096562</pqid></control><display><type>article</type><title>Studies of the collagen fold formation in aqueous solutions of α-gelatin. II</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><creator>Eagland, D. ; Pilling, G.</creator><creatorcontrib>Eagland, D. ; Pilling, G.</creatorcontrib><description>Optical rotation and density studies have been performed as a function of time on solutions of a single‐strand gelatin in salt‐free solutions and in solutions containing sodium bromide, tetramethyl and tetrabutylammonium bromide. The reversion to the collagen fold is shown to be first order in all cases but undergoes a change in magnitude as a function of an aggregation process which occurs at a concentration of approximately 0.1% w/v. The structuring effects of the electrolytes on the solvent are shown to relate to the extent of helix regeneration by the protein, in the presence of the electrolyte. The extent of helix regeneration is also shown to relate to the thickness of the electric double layer surrounding the protein molecule.</description><identifier>ISSN: 0006-3525</identifier><identifier>EISSN: 1097-0282</identifier><identifier>DOI: 10.1002/bip.1980.360190110</identifier><identifier>PMID: 7370393</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Animals ; Collagen ; Gelatin ; Osmolar Concentration ; Protein Conformation ; Rats ; Tendons</subject><ispartof>Biopolymers, 1980-01, Vol.19 (1), p.147-164</ispartof><rights>Copyright © 1980 John Wiley &amp; Sons, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3040-9104c4d4946badcaae26816245b531825e6f80cbf5e6cb5f8baaf254761758ba3</citedby><cites>FETCH-LOGICAL-c3040-9104c4d4946badcaae26816245b531825e6f80cbf5e6cb5f8baaf254761758ba3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbip.1980.360190110$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbip.1980.360190110$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7370393$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Eagland, D.</creatorcontrib><creatorcontrib>Pilling, G.</creatorcontrib><title>Studies of the collagen fold formation in aqueous solutions of α-gelatin. II</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><description>Optical rotation and density studies have been performed as a function of time on solutions of a single‐strand gelatin in salt‐free solutions and in solutions containing sodium bromide, tetramethyl and tetrabutylammonium bromide. The reversion to the collagen fold is shown to be first order in all cases but undergoes a change in magnitude as a function of an aggregation process which occurs at a concentration of approximately 0.1% w/v. The structuring effects of the electrolytes on the solvent are shown to relate to the extent of helix regeneration by the protein, in the presence of the electrolyte. The extent of helix regeneration is also shown to relate to the thickness of the electric double layer surrounding the protein molecule.</description><subject>Animals</subject><subject>Collagen</subject><subject>Gelatin</subject><subject>Osmolar Concentration</subject><subject>Protein Conformation</subject><subject>Rats</subject><subject>Tendons</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMtOg0AYhSdGU2v1BUxMWLkD_7kCiRtttBLrJbGmy8kAQ0UpVAaifSxfxGdykKZx6WZu__nOnByEjjF4GICcxfnKw2EAHhWAQ8AYdtAQQ-i7QAKyi4YAIFzKCd9HB8a8AjBGMQzQwKc-0JAO0d1T06a5Nk6VOc2LdpKqKNRCl05WFald6qVq8qp08tJR762uWuOYqmi7t1_m-8td6MJqSs-JokO0l6nC6KPNPkLP11ez8Y07fZhE44upm1Bg4IYYWMJSFjIRqzRRShMRYEEYjznFAeFaZAEkcWYPScyzIFYqI5z5AvvcXugInfa-q7qyqUwjl7lJtI1edhGlzyEUXBArJL0wqStjap3JVZ0vVb2WGGTXobQdyq5Due3QQicb9zZe6nSLbEqz8_N-_pEXev0PR3kZPf61d3s8N43-3OKqfpPCfsHl_H4i-f1sfhuOsQzoD8i7jZ4</recordid><startdate>198001</startdate><enddate>198001</enddate><creator>Eagland, D.</creator><creator>Pilling, G.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>198001</creationdate><title>Studies of the collagen fold formation in aqueous solutions of α-gelatin. II</title><author>Eagland, D. ; Pilling, G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3040-9104c4d4946badcaae26816245b531825e6f80cbf5e6cb5f8baaf254761758ba3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Animals</topic><topic>Collagen</topic><topic>Gelatin</topic><topic>Osmolar Concentration</topic><topic>Protein Conformation</topic><topic>Rats</topic><topic>Tendons</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Eagland, D.</creatorcontrib><creatorcontrib>Pilling, G.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biopolymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Eagland, D.</au><au>Pilling, G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies of the collagen fold formation in aqueous solutions of α-gelatin. II</atitle><jtitle>Biopolymers</jtitle><addtitle>Biopolymers</addtitle><date>1980-01</date><risdate>1980</risdate><volume>19</volume><issue>1</issue><spage>147</spage><epage>164</epage><pages>147-164</pages><issn>0006-3525</issn><eissn>1097-0282</eissn><abstract>Optical rotation and density studies have been performed as a function of time on solutions of a single‐strand gelatin in salt‐free solutions and in solutions containing sodium bromide, tetramethyl and tetrabutylammonium bromide. The reversion to the collagen fold is shown to be first order in all cases but undergoes a change in magnitude as a function of an aggregation process which occurs at a concentration of approximately 0.1% w/v. The structuring effects of the electrolytes on the solvent are shown to relate to the extent of helix regeneration by the protein, in the presence of the electrolyte. The extent of helix regeneration is also shown to relate to the thickness of the electric double layer surrounding the protein molecule.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>7370393</pmid><doi>10.1002/bip.1980.360190110</doi><tpages>18</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-3525
ispartof Biopolymers, 1980-01, Vol.19 (1), p.147-164
issn 0006-3525
1097-0282
language eng
recordid cdi_proquest_miscellaneous_75096562
source MEDLINE; Wiley Online Library Journals Frontfile Complete
subjects Animals
Collagen
Gelatin
Osmolar Concentration
Protein Conformation
Rats
Tendons
title Studies of the collagen fold formation in aqueous solutions of α-gelatin. II
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T10%3A21%3A50IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Studies%20of%20the%20collagen%20fold%20formation%20in%20aqueous%20solutions%20of%20%CE%B1-gelatin.%20II&rft.jtitle=Biopolymers&rft.au=Eagland,%20D.&rft.date=1980-01&rft.volume=19&rft.issue=1&rft.spage=147&rft.epage=164&rft.pages=147-164&rft.issn=0006-3525&rft.eissn=1097-0282&rft_id=info:doi/10.1002/bip.1980.360190110&rft_dat=%3Cproquest_cross%3E75096562%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=75096562&rft_id=info:pmid/7370393&rfr_iscdi=true