Calorimetric investigations of the helix-coil conversion of phenylalaninespecific transfer ribonucleic acid
The enthalpy of the helix-coil conversion of phenylalaninespecific transfer ribonucleic acid from brewer's yeast (tRNA Phe brewer's yeast) has been measured using both an LKB 10700-2 batch miciocalorimeter and an adiabatic differential scanning calorimeter. In the mixing calorimeter the co...
Gespeichert in:
Veröffentlicht in: | Biophysical chemistry 1974-02, Vol.1 (3), p.214-221 |
---|---|
Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 221 |
---|---|
container_issue | 3 |
container_start_page | 214 |
container_title | Biophysical chemistry |
container_volume | 1 |
creator | Bode, Diedrich Schernau, Ulrich Ackermann, Theodor |
description | The enthalpy of the helix-coil conversion of phenylalaninespecific transfer ribonucleic acid from brewer's yeast (tRNA
Phe
brewer's yeast) has been measured using both an LKB 10700-2 batch miciocalorimeter and an adiabatic differential scanning calorimeter. In the mixing calorimeter the conversion from coil to helix was induced by mixing a tRNA
Phe solution with a solution containing an excess of MgSO
4. We measured the enthalpy of this reaction stepwise in the temperature range from +9 to +60° C. For the enthalpy of folding of tRNA
Phe from coil to helix this method yielded the remarkably high value of −310
kcal
mole
of tRNA
Phe. With the differential scanning calorimeter in which the helix-coil conversion is simply induced by raising the temperature we found a value of +240
kcal
mole
of tRNA
Phe at a
Tm value of 76° C and a value of +200
kcal
mole
of tRNA
Phe at a
T
m value of 50° C. A comparison of the apparent van't Hoff enthalpies with the calorimetrically measured enthalpies shows, that the cooperativity of the system increases continually with rising melting temperatures - which are achieved by increasing Mg
2+ concentrations - reaching a constant value at about 57° C. Above this temperature value the thermodynamic behaviour of the helix-coil conversion of tRNA
Phe may be approximately described by the model of an all-or-none process. |
doi_str_mv | 10.1016/0301-4622(74)80007-4 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_82562484</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0301462274800074</els_id><sourcerecordid>82562484</sourcerecordid><originalsourceid>FETCH-LOGICAL-c272t-5be9568c8514753c7c1e03d6653afd439a399f4937589e92af9e7d3edf2e40263</originalsourceid><addsrcrecordid>eNp9kE9PwyAYh4nRzDn9Bpr0ZPRQpUBLuZiYxX_JEi96Joy-OJSVCe3ivr3ULTt6IuH3vD94H4TOC3xT4KK6xRQXOasIueLsusYY85wdoHFRc5ozgvEhGu-RY3QS42dicAJHaMQqLEosxuhrqpwPdgldsDqz7RpiZz9UZ30bM2-ybgHZApz9ybW3LtM-ESGmdAhXC2g3TjnV2hbiCrQ1qaQLqo0GQhbs3Le9dpAulbbNKToyykU4250T9P748DZ9zmevTy_T-1muCSddXs5BlFWt67JgvKSa6wIwbaqqpMo0jApFhTBMUF7WAgRRRgBvKDSGAMOkohN0ue1dBf_dp4Xk0kYNLv0TfB9lTcqKsJolkG1BHXyMAYxcJRUqbGSB5eBYDgLlIFByJv8cy2HsYtffz5fQ7Id2UlN-t80hLbm2EGTUFloNjQ2gO9l4-_8Dv1cfjO0</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>82562484</pqid></control><display><type>article</type><title>Calorimetric investigations of the helix-coil conversion of phenylalaninespecific transfer ribonucleic acid</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Bode, Diedrich ; Schernau, Ulrich ; Ackermann, Theodor</creator><creatorcontrib>Bode, Diedrich ; Schernau, Ulrich ; Ackermann, Theodor</creatorcontrib><description>The enthalpy of the helix-coil conversion of phenylalaninespecific transfer ribonucleic acid from brewer's yeast (tRNA
Phe
brewer's yeast) has been measured using both an LKB 10700-2 batch miciocalorimeter and an adiabatic differential scanning calorimeter. In the mixing calorimeter the conversion from coil to helix was induced by mixing a tRNA
Phe solution with a solution containing an excess of MgSO
4. We measured the enthalpy of this reaction stepwise in the temperature range from +9 to +60° C. For the enthalpy of folding of tRNA
Phe from coil to helix this method yielded the remarkably high value of −310
kcal
mole
of tRNA
Phe. With the differential scanning calorimeter in which the helix-coil conversion is simply induced by raising the temperature we found a value of +240
kcal
mole
of tRNA
Phe at a
Tm value of 76° C and a value of +200
kcal
mole
of tRNA
Phe at a
T
m value of 50° C. A comparison of the apparent van't Hoff enthalpies with the calorimetrically measured enthalpies shows, that the cooperativity of the system increases continually with rising melting temperatures - which are achieved by increasing Mg
2+ concentrations - reaching a constant value at about 57° C. Above this temperature value the thermodynamic behaviour of the helix-coil conversion of tRNA
Phe may be approximately described by the model of an all-or-none process.</description><identifier>ISSN: 0301-4622</identifier><identifier>EISSN: 1873-4200</identifier><identifier>DOI: 10.1016/0301-4622(74)80007-4</identifier><identifier>PMID: 4609509</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Calorimetry ; Macromolecular Substances ; Magnesium ; Nucleic Acid Conformation ; Phenylalanine ; RNA, Transfer ; Saccharomyces cerevisiae ; Sodium ; Spectrophotometry, Ultraviolet ; Temperature ; Thermodynamics</subject><ispartof>Biophysical chemistry, 1974-02, Vol.1 (3), p.214-221</ispartof><rights>1974</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c272t-5be9568c8514753c7c1e03d6653afd439a399f4937589e92af9e7d3edf2e40263</citedby><cites>FETCH-LOGICAL-c272t-5be9568c8514753c7c1e03d6653afd439a399f4937589e92af9e7d3edf2e40263</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0301-4622(74)80007-4$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4609509$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bode, Diedrich</creatorcontrib><creatorcontrib>Schernau, Ulrich</creatorcontrib><creatorcontrib>Ackermann, Theodor</creatorcontrib><title>Calorimetric investigations of the helix-coil conversion of phenylalaninespecific transfer ribonucleic acid</title><title>Biophysical chemistry</title><addtitle>Biophys Chem</addtitle><description>The enthalpy of the helix-coil conversion of phenylalaninespecific transfer ribonucleic acid from brewer's yeast (tRNA
Phe
brewer's yeast) has been measured using both an LKB 10700-2 batch miciocalorimeter and an adiabatic differential scanning calorimeter. In the mixing calorimeter the conversion from coil to helix was induced by mixing a tRNA
Phe solution with a solution containing an excess of MgSO
4. We measured the enthalpy of this reaction stepwise in the temperature range from +9 to +60° C. For the enthalpy of folding of tRNA
Phe from coil to helix this method yielded the remarkably high value of −310
kcal
mole
of tRNA
Phe. With the differential scanning calorimeter in which the helix-coil conversion is simply induced by raising the temperature we found a value of +240
kcal
mole
of tRNA
Phe at a
Tm value of 76° C and a value of +200
kcal
mole
of tRNA
Phe at a
T
m value of 50° C. A comparison of the apparent van't Hoff enthalpies with the calorimetrically measured enthalpies shows, that the cooperativity of the system increases continually with rising melting temperatures - which are achieved by increasing Mg
2+ concentrations - reaching a constant value at about 57° C. Above this temperature value the thermodynamic behaviour of the helix-coil conversion of tRNA
Phe may be approximately described by the model of an all-or-none process.</description><subject>Calorimetry</subject><subject>Macromolecular Substances</subject><subject>Magnesium</subject><subject>Nucleic Acid Conformation</subject><subject>Phenylalanine</subject><subject>RNA, Transfer</subject><subject>Saccharomyces cerevisiae</subject><subject>Sodium</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Temperature</subject><subject>Thermodynamics</subject><issn>0301-4622</issn><issn>1873-4200</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9PwyAYh4nRzDn9Bpr0ZPRQpUBLuZiYxX_JEi96Joy-OJSVCe3ivr3ULTt6IuH3vD94H4TOC3xT4KK6xRQXOasIueLsusYY85wdoHFRc5ozgvEhGu-RY3QS42dicAJHaMQqLEosxuhrqpwPdgldsDqz7RpiZz9UZ30bM2-ybgHZApz9ybW3LtM-ESGmdAhXC2g3TjnV2hbiCrQ1qaQLqo0GQhbs3Le9dpAulbbNKToyykU4250T9P748DZ9zmevTy_T-1muCSddXs5BlFWt67JgvKSa6wIwbaqqpMo0jApFhTBMUF7WAgRRRgBvKDSGAMOkohN0ue1dBf_dp4Xk0kYNLv0TfB9lTcqKsJolkG1BHXyMAYxcJRUqbGSB5eBYDgLlIFByJv8cy2HsYtffz5fQ7Id2UlN-t80hLbm2EGTUFloNjQ2gO9l4-_8Dv1cfjO0</recordid><startdate>197402</startdate><enddate>197402</enddate><creator>Bode, Diedrich</creator><creator>Schernau, Ulrich</creator><creator>Ackermann, Theodor</creator><general>Elsevier B.V</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>197402</creationdate><title>Calorimetric investigations of the helix-coil conversion of phenylalaninespecific transfer ribonucleic acid</title><author>Bode, Diedrich ; Schernau, Ulrich ; Ackermann, Theodor</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c272t-5be9568c8514753c7c1e03d6653afd439a399f4937589e92af9e7d3edf2e40263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1974</creationdate><topic>Calorimetry</topic><topic>Macromolecular Substances</topic><topic>Magnesium</topic><topic>Nucleic Acid Conformation</topic><topic>Phenylalanine</topic><topic>RNA, Transfer</topic><topic>Saccharomyces cerevisiae</topic><topic>Sodium</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Temperature</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bode, Diedrich</creatorcontrib><creatorcontrib>Schernau, Ulrich</creatorcontrib><creatorcontrib>Ackermann, Theodor</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>Biophysical chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bode, Diedrich</au><au>Schernau, Ulrich</au><au>Ackermann, Theodor</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Calorimetric investigations of the helix-coil conversion of phenylalaninespecific transfer ribonucleic acid</atitle><jtitle>Biophysical chemistry</jtitle><addtitle>Biophys Chem</addtitle><date>1974-02</date><risdate>1974</risdate><volume>1</volume><issue>3</issue><spage>214</spage><epage>221</epage><pages>214-221</pages><issn>0301-4622</issn><eissn>1873-4200</eissn><abstract>The enthalpy of the helix-coil conversion of phenylalaninespecific transfer ribonucleic acid from brewer's yeast (tRNA
Phe
brewer's yeast) has been measured using both an LKB 10700-2 batch miciocalorimeter and an adiabatic differential scanning calorimeter. In the mixing calorimeter the conversion from coil to helix was induced by mixing a tRNA
Phe solution with a solution containing an excess of MgSO
4. We measured the enthalpy of this reaction stepwise in the temperature range from +9 to +60° C. For the enthalpy of folding of tRNA
Phe from coil to helix this method yielded the remarkably high value of −310
kcal
mole
of tRNA
Phe. With the differential scanning calorimeter in which the helix-coil conversion is simply induced by raising the temperature we found a value of +240
kcal
mole
of tRNA
Phe at a
Tm value of 76° C and a value of +200
kcal
mole
of tRNA
Phe at a
T
m value of 50° C. A comparison of the apparent van't Hoff enthalpies with the calorimetrically measured enthalpies shows, that the cooperativity of the system increases continually with rising melting temperatures - which are achieved by increasing Mg
2+ concentrations - reaching a constant value at about 57° C. Above this temperature value the thermodynamic behaviour of the helix-coil conversion of tRNA
Phe may be approximately described by the model of an all-or-none process.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>4609509</pmid><doi>10.1016/0301-4622(74)80007-4</doi><tpages>8</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0301-4622 |
ispartof | Biophysical chemistry, 1974-02, Vol.1 (3), p.214-221 |
issn | 0301-4622 1873-4200 |
language | eng |
recordid | cdi_proquest_miscellaneous_82562484 |
source | MEDLINE; Elsevier ScienceDirect Journals |
subjects | Calorimetry Macromolecular Substances Magnesium Nucleic Acid Conformation Phenylalanine RNA, Transfer Saccharomyces cerevisiae Sodium Spectrophotometry, Ultraviolet Temperature Thermodynamics |
title | Calorimetric investigations of the helix-coil conversion of phenylalaninespecific transfer ribonucleic acid |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T21%3A25%3A59IST&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=Calorimetric%20investigations%20of%20the%20helix-coil%20conversion%20of%20phenylalaninespecific%20transfer%20ribonucleic%20acid&rft.jtitle=Biophysical%20chemistry&rft.au=Bode,%20Diedrich&rft.date=1974-02&rft.volume=1&rft.issue=3&rft.spage=214&rft.epage=221&rft.pages=214-221&rft.issn=0301-4622&rft.eissn=1873-4200&rft_id=info:doi/10.1016/0301-4622(74)80007-4&rft_dat=%3Cproquest_cross%3E82562484%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=82562484&rft_id=info:pmid/4609509&rft_els_id=0301462274800074&rfr_iscdi=true |