Dermatan sulfate and chondroitin 6-sulfate conformations
X-ray diffraction patterns show that dermatan sulfate in oriented, crystalline films occurs as two or three or eight-fold helices. The two-fold helix has a greater axial rise per disaccharide residue [ h = 9.6 A ̊ ] than the corresponding chondroitin 6-sulfate helix [ h = 9.3 A ̊ ] . Three-fold derm...
Gespeichert in:
Veröffentlicht in: | Biochemical and biophysical research communications 1973-10, Vol.54 (4), p.1377-1383 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1383 |
---|---|
container_issue | 4 |
container_start_page | 1377 |
container_title | Biochemical and biophysical research communications |
container_volume | 54 |
creator | Arnott, Struther Guss, J.M. Hukins, D.W.L. Mathews, M.B. |
description | X-ray diffraction patterns show that dermatan sulfate in oriented, crystalline films occurs as two or three or eight-fold helices. The two-fold helix has a greater axial rise per disaccharide residue
[
h
= 9.6
A
̊
]
than the corresponding chondroitin 6-sulfate helix
[
h
= 9.3
A
̊
]
. Three-fold dermatan sulfate and chondroitin 6-sulfate helices both have
h
= 9.5
A
̊
. Consequently the α-L-iduronate residues in dermatan sulfate helices have the C1 chair conformation like β-D-glucuronate in chondroitin 6-sulfate. Since the eight-fold dermatan sulfate helix has
h
= 9.3
A
̊
rather less than the eight-fold chondroitin 6-sulfate helix
[
h
= 9.8
A
̊
]
the possibility of α-L-iduronate 1C chairs cannot be ruled out for it. Computer methods have been used to produce molecular models. In these the polysaccharide chains are almost linear. Each backbone conformation can accommodate a variety of arrangements of charged side groups. |
doi_str_mv | 10.1016/0006-291X(73)91139-X |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_82096770</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0006291X7391139X</els_id><sourcerecordid>82096770</sourcerecordid><originalsourceid>FETCH-LOGICAL-c357t-cb2848c7bb8cc520c4a1819a1f16758a98f24c93f88f11990726badb71488c3a3</originalsourceid><addsrcrecordid>eNp9kE1LxDAQhoMo67r6DxT2JHqoZto0HxdB1k9Y8KKwt5CmCUbaZE1awX9v66579DSH93lnmAehU8BXgIFeY4xplgtYXbDiUgAUIlvtoSlggbMcMNlH0x1yiI5S-sAYgFAxQRPCSsKAThG_M7FVnfLz1DdWdWaufD3X78HXMbjO-TnN_hIdvA0j7YJPx-jAqiaZk-2cobeH-9fFU7Z8eXxe3C4zXZSsy3SVc8I1qyqudZljTRRwEAosUFZyJbjNiRaF5dwCCIFZTitVVwwI57pQxQydb_auY_jsTepk65I2TaO8CX2SPMeCMoYHkGxAHUNK0Vi5jq5V8VsClqMwOdqQow3JCvkrTK6G2tl2f1-1pt6VtoaG_GaTm-HJL2eiTNoZr03totGdrIP7_8APzMZ5_Q</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>82096770</pqid></control><display><type>article</type><title>Dermatan sulfate and chondroitin 6-sulfate conformations</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Arnott, Struther ; Guss, J.M. ; Hukins, D.W.L. ; Mathews, M.B.</creator><creatorcontrib>Arnott, Struther ; Guss, J.M. ; Hukins, D.W.L. ; Mathews, M.B.</creatorcontrib><description>X-ray diffraction patterns show that dermatan sulfate in oriented, crystalline films occurs as two or three or eight-fold helices. The two-fold helix has a greater axial rise per disaccharide residue
[
h
= 9.6
A
̊
]
than the corresponding chondroitin 6-sulfate helix
[
h
= 9.3
A
̊
]
. Three-fold dermatan sulfate and chondroitin 6-sulfate helices both have
h
= 9.5
A
̊
. Consequently the α-L-iduronate residues in dermatan sulfate helices have the C1 chair conformation like β-D-glucuronate in chondroitin 6-sulfate. Since the eight-fold dermatan sulfate helix has
h
= 9.3
A
̊
rather less than the eight-fold chondroitin 6-sulfate helix
[
h
= 9.8
A
̊
]
the possibility of α-L-iduronate 1C chairs cannot be ruled out for it. Computer methods have been used to produce molecular models. In these the polysaccharide chains are almost linear. Each backbone conformation can accommodate a variety of arrangements of charged side groups.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(73)91139-X</identifier><identifier>PMID: 4754716</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Chondroitin ; Models, Chemical ; Molecular Conformation ; Skin ; Sulfates ; Swine ; X-Ray Diffraction</subject><ispartof>Biochemical and biophysical research communications, 1973-10, Vol.54 (4), p.1377-1383</ispartof><rights>1973</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-cb2848c7bb8cc520c4a1819a1f16758a98f24c93f88f11990726badb71488c3a3</citedby><cites>FETCH-LOGICAL-c357t-cb2848c7bb8cc520c4a1819a1f16758a98f24c93f88f11990726badb71488c3a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(73)91139-X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,782,786,3552,27931,27932,46002</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4754716$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Arnott, Struther</creatorcontrib><creatorcontrib>Guss, J.M.</creatorcontrib><creatorcontrib>Hukins, D.W.L.</creatorcontrib><creatorcontrib>Mathews, M.B.</creatorcontrib><title>Dermatan sulfate and chondroitin 6-sulfate conformations</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>X-ray diffraction patterns show that dermatan sulfate in oriented, crystalline films occurs as two or three or eight-fold helices. The two-fold helix has a greater axial rise per disaccharide residue
[
h
= 9.6
A
̊
]
than the corresponding chondroitin 6-sulfate helix
[
h
= 9.3
A
̊
]
. Three-fold dermatan sulfate and chondroitin 6-sulfate helices both have
h
= 9.5
A
̊
. Consequently the α-L-iduronate residues in dermatan sulfate helices have the C1 chair conformation like β-D-glucuronate in chondroitin 6-sulfate. Since the eight-fold dermatan sulfate helix has
h
= 9.3
A
̊
rather less than the eight-fold chondroitin 6-sulfate helix
[
h
= 9.8
A
̊
]
the possibility of α-L-iduronate 1C chairs cannot be ruled out for it. Computer methods have been used to produce molecular models. In these the polysaccharide chains are almost linear. Each backbone conformation can accommodate a variety of arrangements of charged side groups.</description><subject>Animals</subject><subject>Chondroitin</subject><subject>Models, Chemical</subject><subject>Molecular Conformation</subject><subject>Skin</subject><subject>Sulfates</subject><subject>Swine</subject><subject>X-Ray Diffraction</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LxDAQhoMo67r6DxT2JHqoZto0HxdB1k9Y8KKwt5CmCUbaZE1awX9v66579DSH93lnmAehU8BXgIFeY4xplgtYXbDiUgAUIlvtoSlggbMcMNlH0x1yiI5S-sAYgFAxQRPCSsKAThG_M7FVnfLz1DdWdWaufD3X78HXMbjO-TnN_hIdvA0j7YJPx-jAqiaZk-2cobeH-9fFU7Z8eXxe3C4zXZSsy3SVc8I1qyqudZljTRRwEAosUFZyJbjNiRaF5dwCCIFZTitVVwwI57pQxQydb_auY_jsTepk65I2TaO8CX2SPMeCMoYHkGxAHUNK0Vi5jq5V8VsClqMwOdqQow3JCvkrTK6G2tl2f1-1pt6VtoaG_GaTm-HJL2eiTNoZr03totGdrIP7_8APzMZ5_Q</recordid><startdate>19731015</startdate><enddate>19731015</enddate><creator>Arnott, Struther</creator><creator>Guss, J.M.</creator><creator>Hukins, D.W.L.</creator><creator>Mathews, M.B.</creator><general>Elsevier Inc</general><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>19731015</creationdate><title>Dermatan sulfate and chondroitin 6-sulfate conformations</title><author>Arnott, Struther ; Guss, J.M. ; Hukins, D.W.L. ; Mathews, M.B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-cb2848c7bb8cc520c4a1819a1f16758a98f24c93f88f11990726badb71488c3a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Animals</topic><topic>Chondroitin</topic><topic>Models, Chemical</topic><topic>Molecular Conformation</topic><topic>Skin</topic><topic>Sulfates</topic><topic>Swine</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Arnott, Struther</creatorcontrib><creatorcontrib>Guss, J.M.</creatorcontrib><creatorcontrib>Hukins, D.W.L.</creatorcontrib><creatorcontrib>Mathews, M.B.</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Arnott, Struther</au><au>Guss, J.M.</au><au>Hukins, D.W.L.</au><au>Mathews, M.B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dermatan sulfate and chondroitin 6-sulfate conformations</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1973-10-15</date><risdate>1973</risdate><volume>54</volume><issue>4</issue><spage>1377</spage><epage>1383</epage><pages>1377-1383</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>X-ray diffraction patterns show that dermatan sulfate in oriented, crystalline films occurs as two or three or eight-fold helices. The two-fold helix has a greater axial rise per disaccharide residue
[
h
= 9.6
A
̊
]
than the corresponding chondroitin 6-sulfate helix
[
h
= 9.3
A
̊
]
. Three-fold dermatan sulfate and chondroitin 6-sulfate helices both have
h
= 9.5
A
̊
. Consequently the α-L-iduronate residues in dermatan sulfate helices have the C1 chair conformation like β-D-glucuronate in chondroitin 6-sulfate. Since the eight-fold dermatan sulfate helix has
h
= 9.3
A
̊
rather less than the eight-fold chondroitin 6-sulfate helix
[
h
= 9.8
A
̊
]
the possibility of α-L-iduronate 1C chairs cannot be ruled out for it. Computer methods have been used to produce molecular models. In these the polysaccharide chains are almost linear. Each backbone conformation can accommodate a variety of arrangements of charged side groups.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4754716</pmid><doi>10.1016/0006-291X(73)91139-X</doi><tpages>7</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0006-291X |
ispartof | Biochemical and biophysical research communications, 1973-10, Vol.54 (4), p.1377-1383 |
issn | 0006-291X 1090-2104 |
language | eng |
recordid | cdi_proquest_miscellaneous_82096770 |
source | MEDLINE; Access via ScienceDirect (Elsevier) |
subjects | Animals Chondroitin Models, Chemical Molecular Conformation Skin Sulfates Swine X-Ray Diffraction |
title | Dermatan sulfate and chondroitin 6-sulfate conformations |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-05T09%3A40%3A34IST&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=Dermatan%20sulfate%20and%20chondroitin%206-sulfate%20conformations&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Arnott,%20Struther&rft.date=1973-10-15&rft.volume=54&rft.issue=4&rft.spage=1377&rft.epage=1383&rft.pages=1377-1383&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/0006-291X(73)91139-X&rft_dat=%3Cproquest_cross%3E82096770%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=82096770&rft_id=info:pmid/4754716&rft_els_id=0006291X7391139X&rfr_iscdi=true |