Comparative study of human and salmon calcitonin secondary structure in solutions with low dielectric constants
Molecular conformations of salmon (sCT) and human (hCT) calcitonin in media with different concentrations of methanol/water and trifluoroethanol/water have been investigated by fluorescence, circular dichroism (CD) and infrared spectroscopy techniques. In these media, sCT and hCT adopt an alpha-heli...
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| Veröffentlicht in: | The Journal of biological chemistry 1993-03, Vol.268 (9), p.6408-6414 |
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| creator | ARVINTE, T DRAKE, A. F |
| description | Molecular conformations of salmon (sCT) and human (hCT) calcitonin in media with different concentrations of methanol/water
and trifluoroethanol/water have been investigated by fluorescence, circular dichroism (CD) and infrared spectroscopy techniques.
In these media, sCT and hCT adopt an alpha-helical structure comprising up to 40-48% of the amino acids. CD experiments reveal
that for both peptides, the ordering of the Cys1-Cys7 disulfide link and the alpha-helix formation can be distinguished. Disulfide
bond ordering is similar in both calcitonins. sCT adopts the alpha-helical structure more readily than hCT, as solvent polarity
is reduced. In 2,2,2-trifluoroethanol (TFE)/water mixtures the alpha-helix formation for both hCT and sCT is a two-step process.
The first alpha-helix formation step occurs at lower TFE concentrations (less than 11 mol% TFE for hCT and 6 mol% TFE for
sCT). The second alpha-helix formation step represents 50 and 23% of the whole conformational change for hCT and sCT, respectively.
Tyrosine fluorescence measurements correlate with the far ultraviolet CD changes associated with the peptide backbone. hCT
is seen to adopt a left-handed, extended conformation in aqueous media below -50 degrees C. |
| doi_str_mv | 10.1016/S0021-9258(18)53267-1 |
| format | Article |
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and trifluoroethanol/water have been investigated by fluorescence, circular dichroism (CD) and infrared spectroscopy techniques.
In these media, sCT and hCT adopt an alpha-helical structure comprising up to 40-48% of the amino acids. CD experiments reveal
that for both peptides, the ordering of the Cys1-Cys7 disulfide link and the alpha-helix formation can be distinguished. Disulfide
bond ordering is similar in both calcitonins. sCT adopts the alpha-helical structure more readily than hCT, as solvent polarity
is reduced. In 2,2,2-trifluoroethanol (TFE)/water mixtures the alpha-helix formation for both hCT and sCT is a two-step process.
The first alpha-helix formation step occurs at lower TFE concentrations (less than 11 mol% TFE for hCT and 6 mol% TFE for
sCT). The second alpha-helix formation step represents 50 and 23% of the whole conformational change for hCT and sCT, respectively.
Tyrosine fluorescence measurements correlate with the far ultraviolet CD changes associated with the peptide backbone. hCT
is seen to adopt a left-handed, extended conformation in aqueous media below -50 degrees C.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)53267-1</identifier><identifier>PMID: 8454613</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Aminoacids, peptides. Hormones. Neuropeptides ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; C.D ; calcitonin ; Calcitonin - chemistry ; Circular Dichroism ; comparative studies ; Fundamental and applied biological sciences. Psychology ; hormones ; Humans ; man ; Marine ; Methanol - chemistry ; Molecular Sequence Data ; molecular structure ; peptides ; Protein Structure, Secondary ; Proteins ; Salmo salar ; Salmon ; secondary structure ; Solutions ; Solvents ; Spectrometry, Fluorescence ; Trifluoroethanol - chemistry ; Water - chemistry</subject><ispartof>The Journal of biological chemistry, 1993-03, Vol.268 (9), p.6408-6414</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c438t-573432c7272a0ec3b521dd3f701e4b20c04db5508ad2e4885c112ac57cb1e60a3</citedby><cites>FETCH-LOGICAL-c438t-573432c7272a0ec3b521dd3f701e4b20c04db5508ad2e4885c112ac57cb1e60a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4727307$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8454613$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>ARVINTE, T</creatorcontrib><creatorcontrib>DRAKE, A. F</creatorcontrib><title>Comparative study of human and salmon calcitonin secondary structure in solutions with low dielectric constants</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Molecular conformations of salmon (sCT) and human (hCT) calcitonin in media with different concentrations of methanol/water
and trifluoroethanol/water have been investigated by fluorescence, circular dichroism (CD) and infrared spectroscopy techniques.
In these media, sCT and hCT adopt an alpha-helical structure comprising up to 40-48% of the amino acids. CD experiments reveal
that for both peptides, the ordering of the Cys1-Cys7 disulfide link and the alpha-helix formation can be distinguished. Disulfide
bond ordering is similar in both calcitonins. sCT adopts the alpha-helical structure more readily than hCT, as solvent polarity
is reduced. In 2,2,2-trifluoroethanol (TFE)/water mixtures the alpha-helix formation for both hCT and sCT is a two-step process.
The first alpha-helix formation step occurs at lower TFE concentrations (less than 11 mol% TFE for hCT and 6 mol% TFE for
sCT). The second alpha-helix formation step represents 50 and 23% of the whole conformational change for hCT and sCT, respectively.
Tyrosine fluorescence measurements correlate with the far ultraviolet CD changes associated with the peptide backbone. hCT
is seen to adopt a left-handed, extended conformation in aqueous media below -50 degrees C.</description><subject>Amino Acid Sequence</subject><subject>Aminoacids, peptides. Hormones. Neuropeptides</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>C.D</subject><subject>calcitonin</subject><subject>Calcitonin - chemistry</subject><subject>Circular Dichroism</subject><subject>comparative studies</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hormones</subject><subject>Humans</subject><subject>man</subject><subject>Marine</subject><subject>Methanol - chemistry</subject><subject>Molecular Sequence Data</subject><subject>molecular structure</subject><subject>peptides</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Salmo salar</subject><subject>Salmon</subject><subject>secondary structure</subject><subject>Solutions</subject><subject>Solvents</subject><subject>Spectrometry, Fluorescence</subject><subject>Trifluoroethanol - chemistry</subject><subject>Water - chemistry</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2KFDEUhYMoYzv6CANBRHRRmpu_Si-Hxj8YcKGCu5BKUlakKmmTlM28venpprdmE8j9Ti6cD6EbIO-AgHz_jRAK3ZYK9QbUW8Go7Dt4hDZAFOuYgJ-P0eaCPEXPSvlN2uFbuEJXigsugW1Q2qVlb7Kp4a_Hpa7uHqcRT-tiIjbR4WLmJUVszWxDTTFEXLxN0Zl83_C82rpmj4_PaV5rSLHgQ6gTntMBu-Bnb2sOFrdIqSbW8hw9Gc1c_IvzfY1-fPzwffe5u_v66cvu9q6znKnaiZ5xRm1Pe2qIt2wQFJxjY0_A84ESS7gbhCDKOOq5UsICUGNFbwfwkhh2jV6f_t3n9Gf1peolFOvn2USf1qJ7ITkIYP8FQUqQPYUGihNocyol-1Hvc1haDxqIPhrRD0b0sW4NSj8Y0cfczXnBOizeXVJnBW3-6jw3pdU8ZhNtKBeMtw4Y6Rv28oRN4dd0CNnrISQ7-UVTqfRWS968_wPNv6Cp</recordid><startdate>19930325</startdate><enddate>19930325</enddate><creator>ARVINTE, T</creator><creator>DRAKE, A. F</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</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>7QL</scope><scope>7QP</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19930325</creationdate><title>Comparative study of human and salmon calcitonin secondary structure in solutions with low dielectric constants</title><author>ARVINTE, T ; DRAKE, A. F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-573432c7272a0ec3b521dd3f701e4b20c04db5508ad2e4885c112ac57cb1e60a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Aminoacids, peptides. Hormones. Neuropeptides</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>C.D</topic><topic>calcitonin</topic><topic>Calcitonin - chemistry</topic><topic>Circular Dichroism</topic><topic>comparative studies</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hormones</topic><topic>Humans</topic><topic>man</topic><topic>Marine</topic><topic>Methanol - chemistry</topic><topic>Molecular Sequence Data</topic><topic>molecular structure</topic><topic>peptides</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Salmo salar</topic><topic>Salmon</topic><topic>secondary structure</topic><topic>Solutions</topic><topic>Solvents</topic><topic>Spectrometry, Fluorescence</topic><topic>Trifluoroethanol - chemistry</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ARVINTE, T</creatorcontrib><creatorcontrib>DRAKE, A. F</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>ARVINTE, T</au><au>DRAKE, A. F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative study of human and salmon calcitonin secondary structure in solutions with low dielectric constants</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-03-25</date><risdate>1993</risdate><volume>268</volume><issue>9</issue><spage>6408</spage><epage>6414</epage><pages>6408-6414</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Molecular conformations of salmon (sCT) and human (hCT) calcitonin in media with different concentrations of methanol/water
and trifluoroethanol/water have been investigated by fluorescence, circular dichroism (CD) and infrared spectroscopy techniques.
In these media, sCT and hCT adopt an alpha-helical structure comprising up to 40-48% of the amino acids. CD experiments reveal
that for both peptides, the ordering of the Cys1-Cys7 disulfide link and the alpha-helix formation can be distinguished. Disulfide
bond ordering is similar in both calcitonins. sCT adopts the alpha-helical structure more readily than hCT, as solvent polarity
is reduced. In 2,2,2-trifluoroethanol (TFE)/water mixtures the alpha-helix formation for both hCT and sCT is a two-step process.
The first alpha-helix formation step occurs at lower TFE concentrations (less than 11 mol% TFE for hCT and 6 mol% TFE for
sCT). The second alpha-helix formation step represents 50 and 23% of the whole conformational change for hCT and sCT, respectively.
Tyrosine fluorescence measurements correlate with the far ultraviolet CD changes associated with the peptide backbone. hCT
is seen to adopt a left-handed, extended conformation in aqueous media below -50 degrees C.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8454613</pmid><doi>10.1016/S0021-9258(18)53267-1</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1993-03, Vol.268 (9), p.6408-6414 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Animals Biological and medical sciences C.D calcitonin Calcitonin - chemistry Circular Dichroism comparative studies Fundamental and applied biological sciences. Psychology hormones Humans man Marine Methanol - chemistry Molecular Sequence Data molecular structure peptides Protein Structure, Secondary Proteins Salmo salar Salmon secondary structure Solutions Solvents Spectrometry, Fluorescence Trifluoroethanol - chemistry Water - chemistry |
| title | Comparative study of human and salmon calcitonin secondary structure in solutions with low dielectric constants |
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