The structure of hemopeptide 1–65 from cytochrome c
Hemopeptide 1–65 was cleaved from horse heart cytochrome c by cyanogen bromide and purified by exclusion chromatography. Although the intrinsic viscosity of the hemopeptide is intermediate between that of a compact sphere and a random coil, the ultraviolet circular dichroic spectrum indicates no sig...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1972, Vol.148 (1), p.141-147 |
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| container_title | Archives of biochemistry and biophysics |
| container_volume | 148 |
| creator | Babul, Jorge McGowan, Eleanor B. Stellwagen, Earle |
| description | Hemopeptide 1–65 was cleaved from horse heart cytochrome
c by cyanogen bromide and purified by exclusion chromatography. Although the intrinsic viscosity of the hemopeptide is intermediate between that of a compact sphere and a random coil, the ultraviolet circular dichroic spectrum indicates no significant amount of secondary structure. A variety of chemical and spectral measurements indicate that two histidyl residues of the hemopeptide are coordinated with the heme iron, that the indole ring of tryptophan 59 is one-third exposed, that the heme moiety is two-thirds exposed, and that tyrosyl 48 and the third histidyl residue are completely exposed. It was concluded that the hemopeptide has a relatively open conformation quite different from its conformation in the native protein. |
| doi_str_mv | 10.1016/0003-9861(72)90124-5 |
| format | Article |
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c by cyanogen bromide and purified by exclusion chromatography. Although the intrinsic viscosity of the hemopeptide is intermediate between that of a compact sphere and a random coil, the ultraviolet circular dichroic spectrum indicates no significant amount of secondary structure. A variety of chemical and spectral measurements indicate that two histidyl residues of the hemopeptide are coordinated with the heme iron, that the indole ring of tryptophan 59 is one-third exposed, that the heme moiety is two-thirds exposed, and that tyrosyl 48 and the third histidyl residue are completely exposed. It was concluded that the hemopeptide has a relatively open conformation quite different from its conformation in the native protein.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(72)90124-5</identifier><identifier>PMID: 5062022</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetates ; Alkylation ; Amino Acids - analysis ; Animals ; Bromine ; Chemical Phenomena ; Chemistry, Physical ; Chromatography, Gel ; Circular Dichroism ; Cyanogen Bromide ; Cytochromes - analysis ; Heme - analysis ; Histidine ; Horses ; Myocardium ; Peptides - analysis ; Peptides - isolation & purification ; Potassium Iodide ; Protein Binding ; Protein Conformation ; Spectrophotometry ; Ultracentrifugation ; Ultraviolet Rays ; Viscosity</subject><ispartof>Archives of biochemistry and biophysics, 1972, Vol.148 (1), p.141-147</ispartof><rights>1972</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-c7d6f0eb5d7a73f1164febca47561b08163b41ce39f00df4066d99f5197111373</citedby><cites>FETCH-LOGICAL-c357t-c7d6f0eb5d7a73f1164febca47561b08163b41ce39f00df4066d99f5197111373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986172901245$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5062022$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Babul, Jorge</creatorcontrib><creatorcontrib>McGowan, Eleanor B.</creatorcontrib><creatorcontrib>Stellwagen, Earle</creatorcontrib><title>The structure of hemopeptide 1–65 from cytochrome c</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Hemopeptide 1–65 was cleaved from horse heart cytochrome
c by cyanogen bromide and purified by exclusion chromatography. Although the intrinsic viscosity of the hemopeptide is intermediate between that of a compact sphere and a random coil, the ultraviolet circular dichroic spectrum indicates no significant amount of secondary structure. A variety of chemical and spectral measurements indicate that two histidyl residues of the hemopeptide are coordinated with the heme iron, that the indole ring of tryptophan 59 is one-third exposed, that the heme moiety is two-thirds exposed, and that tyrosyl 48 and the third histidyl residue are completely exposed. It was concluded that the hemopeptide has a relatively open conformation quite different from its conformation in the native protein.</description><subject>Acetates</subject><subject>Alkylation</subject><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Bromine</subject><subject>Chemical Phenomena</subject><subject>Chemistry, Physical</subject><subject>Chromatography, Gel</subject><subject>Circular Dichroism</subject><subject>Cyanogen Bromide</subject><subject>Cytochromes - analysis</subject><subject>Heme - analysis</subject><subject>Histidine</subject><subject>Horses</subject><subject>Myocardium</subject><subject>Peptides - analysis</subject><subject>Peptides - isolation & purification</subject><subject>Potassium Iodide</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Spectrophotometry</subject><subject>Ultracentrifugation</subject><subject>Ultraviolet Rays</subject><subject>Viscosity</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1972</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1Kw0AQxxdRaq2-gUJOoofoTDa7m70IUvyCgpd6XpLNLI00TdxNhN58B9_QJzG1pUdPM_D_GObH2DnCDQLKWwDgsc4kXqnkWgMmaSwO2BhByxh4lh6y8d5yzE5CeAdATGUyYiMBMoEkGTMxX1AUOt_brvcUNS5aUN201HZVSRH-fH1LETnf1JFdd41dDBtF9pQduXwZ6Gw3J-zt8WE-fY5nr08v0_tZbLlQXWxVKR1QIUqVK-4QZeqosHmqhMQCMpS8SNES1w6gdClIWWrtBGqFiFzxCbvc9ra--egpdKaugqXlMl9R0weTIZdaahiM6dZofROCJ2daX9W5XxsEs6FlNijMBoVRifmjZcQQu9j190VN5T60wzPod1udhic_K_Im2IpWlsrKk-1M2VT_H_gFQjV3qA</recordid><startdate>1972</startdate><enddate>1972</enddate><creator>Babul, Jorge</creator><creator>McGowan, Eleanor B.</creator><creator>Stellwagen, Earle</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>1972</creationdate><title>The structure of hemopeptide 1–65 from cytochrome c</title><author>Babul, Jorge ; McGowan, Eleanor B. ; Stellwagen, Earle</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-c7d6f0eb5d7a73f1164febca47561b08163b41ce39f00df4066d99f5197111373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1972</creationdate><topic>Acetates</topic><topic>Alkylation</topic><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Bromine</topic><topic>Chemical Phenomena</topic><topic>Chemistry, Physical</topic><topic>Chromatography, Gel</topic><topic>Circular Dichroism</topic><topic>Cyanogen Bromide</topic><topic>Cytochromes - analysis</topic><topic>Heme - analysis</topic><topic>Histidine</topic><topic>Horses</topic><topic>Myocardium</topic><topic>Peptides - analysis</topic><topic>Peptides - isolation & purification</topic><topic>Potassium Iodide</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Spectrophotometry</topic><topic>Ultracentrifugation</topic><topic>Ultraviolet Rays</topic><topic>Viscosity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Babul, Jorge</creatorcontrib><creatorcontrib>McGowan, Eleanor B.</creatorcontrib><creatorcontrib>Stellwagen, Earle</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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Babul, Jorge</au><au>McGowan, Eleanor B.</au><au>Stellwagen, Earle</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The structure of hemopeptide 1–65 from cytochrome c</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1972</date><risdate>1972</risdate><volume>148</volume><issue>1</issue><spage>141</spage><epage>147</epage><pages>141-147</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Hemopeptide 1–65 was cleaved from horse heart cytochrome
c by cyanogen bromide and purified by exclusion chromatography. Although the intrinsic viscosity of the hemopeptide is intermediate between that of a compact sphere and a random coil, the ultraviolet circular dichroic spectrum indicates no significant amount of secondary structure. A variety of chemical and spectral measurements indicate that two histidyl residues of the hemopeptide are coordinated with the heme iron, that the indole ring of tryptophan 59 is one-third exposed, that the heme moiety is two-thirds exposed, and that tyrosyl 48 and the third histidyl residue are completely exposed. It was concluded that the hemopeptide has a relatively open conformation quite different from its conformation in the native protein.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>5062022</pmid><doi>10.1016/0003-9861(72)90124-5</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1972, Vol.148 (1), p.141-147 |
| issn | 0003-9861 1096-0384 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Acetates Alkylation Amino Acids - analysis Animals Bromine Chemical Phenomena Chemistry, Physical Chromatography, Gel Circular Dichroism Cyanogen Bromide Cytochromes - analysis Heme - analysis Histidine Horses Myocardium Peptides - analysis Peptides - isolation & purification Potassium Iodide Protein Binding Protein Conformation Spectrophotometry Ultracentrifugation Ultraviolet Rays Viscosity |
| title | The structure of hemopeptide 1–65 from cytochrome c |
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