Quantitative study of secondary structure of histones H1, H2A, and H4 in solution by infrared spectroscopy
The secondary structure of histories H1, H2A, and H4 (F1, F2a2, and F2a1) has been quantitatively studied in heavy water (2H2O) solutions in a wide range of histone concentration, p2H, and concentration of sodium chloride using an improved infrared spectroscopy method. Under all conditions there are...
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| Veröffentlicht in: | European journal of biochemistry 1976-08, Vol.67 (1), p.123-128 |
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| container_end_page | 128 |
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| container_issue | 1 |
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| container_title | European journal of biochemistry |
| container_volume | 67 |
| creator | Shestapalov, B.V Chirgadze, YU.N |
| description | The secondary structure of histories H1, H2A, and H4 (F1, F2a2, and F2a1) has been quantitatively studied in heavy water (2H2O) solutions in a wide range of histone concentration, p2H, and concentration of sodium chloride using an improved infrared spectroscopy method. Under all conditions there are about 5–10% of α helix. Conditions favourable for aggregation induce formation of antiparallel pleated sheet structure to an extent of about 15% in H1 and H2A and about 30% in H4. When the p2H and concentration of NaCl are in the physiological range, there is the sane content of this structure in H2A and H4 and none in HI. |
| doi_str_mv | 10.1111/j.1432-1033.1976.tb10640.x |
| format | Article |
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Under all conditions there are about 5–10% of α helix. Conditions favourable for aggregation induce formation of antiparallel pleated sheet structure to an extent of about 15% in H1 and H2A and about 30% in H4. When the p2H and concentration of NaCl are in the physiological range, there is the sane content of this structure in H2A and H4 and none in HI.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1976.tb10640.x</identifier><identifier>PMID: 9273</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>animal science ; Animals ; Binding Sites ; calves ; Cattle ; Histones ; Hydrogen-Ion Concentration ; livestock ; Protein Binding ; Protein Conformation ; Sodium Chloride ; Space life sciences ; Spectrophotometry, Infrared ; Thymus Gland ; zoology</subject><ispartof>European journal of biochemistry, 1976-08, Vol.67 (1), p.123-128</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3913-dbceb48d72d9047d790ac6c13eafd330fd65abbcfeb73ed38f14cd2b274f068b3</citedby><cites>FETCH-LOGICAL-c3913-dbceb48d72d9047d790ac6c13eafd330fd65abbcfeb73ed38f14cd2b274f068b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9273$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shestapalov, B.V</creatorcontrib><creatorcontrib>Chirgadze, YU.N</creatorcontrib><title>Quantitative study of secondary structure of histones H1, H2A, and H4 in solution by infrared spectroscopy</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The secondary structure of histories H1, H2A, and H4 (F1, F2a2, and F2a1) has been quantitatively studied in heavy water (2H2O) solutions in a wide range of histone concentration, p2H, and concentration of sodium chloride using an improved infrared spectroscopy method. Under all conditions there are about 5–10% of α helix. Conditions favourable for aggregation induce formation of antiparallel pleated sheet structure to an extent of about 15% in H1 and H2A and about 30% in H4. When the p2H and concentration of NaCl are in the physiological range, there is the sane content of this structure in H2A and H4 and none in HI.</description><subject>animal science</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>calves</subject><subject>Cattle</subject><subject>Histones</subject><subject>Hydrogen-Ion Concentration</subject><subject>livestock</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Sodium Chloride</subject><subject>Space life sciences</subject><subject>Spectrophotometry, Infrared</subject><subject>Thymus Gland</subject><subject>zoology</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkEtv1DAUhS1UBEPhD7DBYsGqCdePcSZsqlK1DFIlhErXlp_gUSYebAeaf4-jGXWPN5bPuffc6w-h9wRaUs_HXUs4ow0BxlrSd6ItmoDg0D4-Q6sn6wytAAhvaL8WL9GrnHcAIHrRvUBnPe3YCu2-T2osoagS_jicy2RnHD3OzsTRqjRXKU2mTMkt8q-QSxxdxltygbf06gKr0eItx2HEOQ5TCXHEeq5Pn1RyFueDMyXFbOJhfo2eezVk9-Z0n6OH25sf19vm7tuXr9dXd41hPWGN1cZpvrEdtT3wznY9KCMMYU55yxh4K9ZKa-Od7pizbOMJN5Zq2nEPYqPZOfpwzD2k-Htyuch9yMYNgxpdnLLcsDWrDEgt_HQsNHXDnJyXhxT29dOSgFwoy51cUMoFpVwoyxNl-Vib356mTHrv7FPrgrWal0fzbxjc_B-x8vbm8z2hS8K7Y4JXUaqfKWT5cE-BMGAgKHDG_gHzrJdw</recordid><startdate>197608</startdate><enddate>197608</enddate><creator>Shestapalov, B.V</creator><creator>Chirgadze, YU.N</creator><general>Blackwell Publishing Ltd</general><scope>FBQ</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>197608</creationdate><title>Quantitative study of secondary structure of histones H1, H2A, and H4 in solution by infrared spectroscopy</title><author>Shestapalov, B.V ; Chirgadze, YU.N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3913-dbceb48d72d9047d790ac6c13eafd330fd65abbcfeb73ed38f14cd2b274f068b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>animal science</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>calves</topic><topic>Cattle</topic><topic>Histones</topic><topic>Hydrogen-Ion Concentration</topic><topic>livestock</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Sodium Chloride</topic><topic>Space life sciences</topic><topic>Spectrophotometry, Infrared</topic><topic>Thymus Gland</topic><topic>zoology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shestapalov, B.V</creatorcontrib><creatorcontrib>Chirgadze, YU.N</creatorcontrib><collection>AGRIS</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>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shestapalov, B.V</au><au>Chirgadze, YU.N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quantitative study of secondary structure of histones H1, H2A, and H4 in solution by infrared spectroscopy</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1976-08</date><risdate>1976</risdate><volume>67</volume><issue>1</issue><spage>123</spage><epage>128</epage><pages>123-128</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>The secondary structure of histories H1, H2A, and H4 (F1, F2a2, and F2a1) has been quantitatively studied in heavy water (2H2O) solutions in a wide range of histone concentration, p2H, and concentration of sodium chloride using an improved infrared spectroscopy method. Under all conditions there are about 5–10% of α helix. Conditions favourable for aggregation induce formation of antiparallel pleated sheet structure to an extent of about 15% in H1 and H2A and about 30% in H4. When the p2H and concentration of NaCl are in the physiological range, there is the sane content of this structure in H2A and H4 and none in HI.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>9273</pmid><doi>10.1111/j.1432-1033.1976.tb10640.x</doi><tpages>6</tpages></addata></record> |
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| ispartof | European journal of biochemistry, 1976-08, Vol.67 (1), p.123-128 |
| issn | 0014-2956 1432-1033 |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | animal science Animals Binding Sites calves Cattle Histones Hydrogen-Ion Concentration livestock Protein Binding Protein Conformation Sodium Chloride Space life sciences Spectrophotometry, Infrared Thymus Gland zoology |
| title | Quantitative study of secondary structure of histones H1, H2A, and H4 in solution by infrared spectroscopy |
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