Protein-cationic detergent interaction. Fourier transform infrared and laser Raman spectroscopic studies on the interaction between proteins and dodecylpyridinium bromide
Fourier transform infrared and laser Raman spectroscopies were used to study the effects of dodecylpyridinium bromide on the conformation of haemoglobin, myoglobin, bovine serum albumin, ribonuclease, ovalbumin, lysozyme, trypsin and beta-lactoglobulin in aqueous solution. Addition of the cationic d...
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Veröffentlicht in: | Acta biochimica polonica 1979, Vol.26 (3), p.205-214 |
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description | Fourier transform infrared and laser Raman spectroscopies were used to study the effects of dodecylpyridinium bromide on the conformation of haemoglobin, myoglobin, bovine serum albumin, ribonuclease, ovalbumin, lysozyme, trypsin and beta-lactoglobulin in aqueous solution. Addition of the cationic detergent caused a decrease in alpha-helix conformation in highly helical proteins. At low detergent concentrations stabilization of beta-sheet conformation was observed. |
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Fourier transform infrared and laser Raman spectroscopic studies on the interaction between proteins and dodecylpyridinium bromide</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Wasylewski, Z</creator><creatorcontrib>Wasylewski, Z</creatorcontrib><description>Fourier transform infrared and laser Raman spectroscopies were used to study the effects of dodecylpyridinium bromide on the conformation of haemoglobin, myoglobin, bovine serum albumin, ribonuclease, ovalbumin, lysozyme, trypsin and beta-lactoglobulin in aqueous solution. Addition of the cationic detergent caused a decrease in alpha-helix conformation in highly helical proteins. At low detergent concentrations stabilization of beta-sheet conformation was observed.</description><identifier>ISSN: 0001-527X</identifier><identifier>PMID: 494944</identifier><language>eng</language><publisher>Poland</publisher><subject>Cations ; Detergents ; Fourier Analysis ; Protein Conformation - drug effects ; Proteins ; Pyridinium Compounds ; Spectrum Analysis, Raman</subject><ispartof>Acta biochimica polonica, 1979, Vol.26 (3), p.205-214</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/494944$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wasylewski, Z</creatorcontrib><title>Protein-cationic detergent interaction. Fourier transform infrared and laser Raman spectroscopic studies on the interaction between proteins and dodecylpyridinium bromide</title><title>Acta biochimica polonica</title><addtitle>Acta Biochim Pol</addtitle><description>Fourier transform infrared and laser Raman spectroscopies were used to study the effects of dodecylpyridinium bromide on the conformation of haemoglobin, myoglobin, bovine serum albumin, ribonuclease, ovalbumin, lysozyme, trypsin and beta-lactoglobulin in aqueous solution. Addition of the cationic detergent caused a decrease in alpha-helix conformation in highly helical proteins. At low detergent concentrations stabilization of beta-sheet conformation was observed.</description><subject>Cations</subject><subject>Detergents</subject><subject>Fourier Analysis</subject><subject>Protein Conformation - drug effects</subject><subject>Proteins</subject><subject>Pyridinium Compounds</subject><subject>Spectrum Analysis, Raman</subject><issn>0001-527X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkM1KxDAUhbvwbxx9AxdZuaukTdI2SxkcFQYUUXBX8nOrkSapSYrMK_mURmcWchf3cs7h43APigXGuCpZ3b6eFKcxfmBck4rT4-KI8jx0UXw_Bp_AuFKJZLwzCmlIEN7AJWRcvoT61a_Q2s_BQEApCBcHH2y2hyACaCScRqOI2XwSVjgUJ1Ap-Kj8lHkxzdpARN6h9A7_oUhC-gJwaNp1iH8k7TWo7Thtg9HGmdkiGbw1Gs6Kw0GMEc73e1m8rG-eV3fl5uH2fnW9Kacas1QCga5hDeEMdxyU5m1NZYMHKrHqatZxTKGRUks8DKpmlMh2aCTjlZIdZkSQZXG54-ZanzPE1FsTFYyjcODn2Lc053jb5ODFPjhLC7qfgrEibPvdb8kPtbt6ZA</recordid><startdate>1979</startdate><enddate>1979</enddate><creator>Wasylewski, Z</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>1979</creationdate><title>Protein-cationic detergent interaction. 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Fourier transform infrared and laser Raman spectroscopic studies on the interaction between proteins and dodecylpyridinium bromide</atitle><jtitle>Acta biochimica polonica</jtitle><addtitle>Acta Biochim Pol</addtitle><date>1979</date><risdate>1979</risdate><volume>26</volume><issue>3</issue><spage>205</spage><epage>214</epage><pages>205-214</pages><issn>0001-527X</issn><abstract>Fourier transform infrared and laser Raman spectroscopies were used to study the effects of dodecylpyridinium bromide on the conformation of haemoglobin, myoglobin, bovine serum albumin, ribonuclease, ovalbumin, lysozyme, trypsin and beta-lactoglobulin in aqueous solution. Addition of the cationic detergent caused a decrease in alpha-helix conformation in highly helical proteins. At low detergent concentrations stabilization of beta-sheet conformation was observed.</abstract><cop>Poland</cop><pmid>494944</pmid><tpages>10</tpages></addata></record> |
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subjects | Cations Detergents Fourier Analysis Protein Conformation - drug effects Proteins Pyridinium Compounds Spectrum Analysis, Raman |
title | Protein-cationic detergent interaction. Fourier transform infrared and laser Raman spectroscopic studies on the interaction between proteins and dodecylpyridinium bromide |
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