Kinetics of Intermolecular Interaction during Protein Folding of Reduced Cytochrome c
Kinetics of intermolecular interaction between reduced cytochrome c (Cyt c) protein and solvent during the protein-refolding process is studied by monitoring the time dependence of apparent diffusion coefficient ( D) using the pulsed-laser-induced transient grating technique. The refolding was trigg...
Gespeichert in:
| Veröffentlicht in: | Biophysical journal 2004-10, Vol.87 (4), p.2663-2675 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2675 |
|---|---|
| container_issue | 4 |
| container_start_page | 2663 |
| container_title | Biophysical journal |
| container_volume | 87 |
| creator | Nishida, Shinpei Nada, Tomokazu Terazima, Masahide |
| description | Kinetics of intermolecular interaction between reduced cytochrome
c (Cyt
c) protein and solvent during the protein-refolding process is studied by monitoring the time dependence of apparent diffusion coefficient (
D) using the pulsed-laser-induced transient grating technique. The refolding was triggered by photoinduced reduction of unfolded Fe(III) Cyt
c in 3.5
M guanidine hydrochloride (GdnHCl) solution and the change in the diffusion coefficient was monitored in time domain. The relationship between
D and the protein conformations under equilibrium condition were investigated at various GdnHCl concentrations using a photolabeling reagent. The time dependence of the observed transient grating signal was analyzed using these data and two models: a continuous change model of the intermolecular interaction and a two-state model. It was found that the TG signals in various time ranges can be consistently reproduced well by the two-state model. The dynamics of
D is expressed well by a single exponential function with a rate constant of 22
±
7
s
−1 in a whole time range. The folding process of Cyt
c is discussed based on these observations. |
| doi_str_mv | 10.1529/biophysj.104.042531 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1304685</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006349504737376</els_id><sourcerecordid>724443351</sourcerecordid><originalsourceid>FETCH-LOGICAL-c550t-cb12d837d0afde1b9d99961473c00e6397303476780ed6ab7952f65a8912b1273</originalsourceid><addsrcrecordid>eNp9kU1v1DAQhi0EotvCL0BCEQduWcafSQ4goRUtFZVAiJ4tx550vcrai51U2n-PqyyfB07W2M_7emZeQl5QWFPJuje9j4ftMe_WFMQaBJOcPiIrKgWrAVr1mKwAQNVcdPKMnOe8A6BMAn1KzgokhVB0RW4_-YCTt7mKQ3UdJkz7OKKdR5OW0tjJx1C5OflwV31JcUIfqss4uoe6iL6imy26anOcot2muMfKPiNPBjNmfH46L8jt5Ydvm4_1zeer6837m9pKCVNte8pcyxsHZnBI-851XaeoaLgFQMW7hgMXjWpaQKdM33SSDUqatqOsSBt-Qd4tvoe536OzGKZkRn1Ifm_SUUfj9d8vwW_1XbzXlINQrSwGr08GKX6fMU9677PFcTQB45y1Uh1jpZ8CvvoH3MU5hTKcZlQ2FKhQBeILZFPMOeHwqxMK-iEz_TOzciH0kllRvfxziN-aU0gFeLsAWFZ57zHpbD2GsnSf0E7aRf_fD34A0oOqKA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>215710146</pqid></control><display><type>article</type><title>Kinetics of Intermolecular Interaction during Protein Folding of Reduced Cytochrome c</title><source>MEDLINE</source><source>Cell Press Free Archives</source><source>Elsevier ScienceDirect Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Nishida, Shinpei ; Nada, Tomokazu ; Terazima, Masahide</creator><creatorcontrib>Nishida, Shinpei ; Nada, Tomokazu ; Terazima, Masahide</creatorcontrib><description>Kinetics of intermolecular interaction between reduced cytochrome
c (Cyt
c) protein and solvent during the protein-refolding process is studied by monitoring the time dependence of apparent diffusion coefficient (
D) using the pulsed-laser-induced transient grating technique. The refolding was triggered by photoinduced reduction of unfolded Fe(III) Cyt
c in 3.5
M guanidine hydrochloride (GdnHCl) solution and the change in the diffusion coefficient was monitored in time domain. The relationship between
D and the protein conformations under equilibrium condition were investigated at various GdnHCl concentrations using a photolabeling reagent. The time dependence of the observed transient grating signal was analyzed using these data and two models: a continuous change model of the intermolecular interaction and a two-state model. It was found that the TG signals in various time ranges can be consistently reproduced well by the two-state model. The dynamics of
D is expressed well by a single exponential function with a rate constant of 22
±
7
s
−1 in a whole time range. The folding process of Cyt
c is discussed based on these observations.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1529/biophysj.104.042531</identifier><identifier>PMID: 15454461</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Biochemistry ; Carbon Monoxide - chemistry ; Computer Simulation ; Cytochromes c - chemistry ; Diffusion ; Elasticity ; Entropy ; Enzyme Activation ; Enzyme Stability ; Guanidine - chemistry ; Hydrogen-Ion Concentration ; Kinetics ; Macromolecular Substances - chemistry ; Models, Chemical ; Oxidation-Reduction ; Protein Binding ; Protein Conformation ; Protein Denaturation ; Protein Folding ; Proteins ; Reaction kinetics ; Solutions ; Solvents - chemistry ; Thermodynamics</subject><ispartof>Biophysical journal, 2004-10, Vol.87 (4), p.2663-2675</ispartof><rights>2004 The Biophysical Society</rights><rights>Copyright 2004 Biophysical Society</rights><rights>Copyright Biophysical Society Oct 2004</rights><rights>Copyright © 2004, Biophysical Society 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c550t-cb12d837d0afde1b9d99961473c00e6397303476780ed6ab7952f65a8912b1273</citedby><cites>FETCH-LOGICAL-c550t-cb12d837d0afde1b9d99961473c00e6397303476780ed6ab7952f65a8912b1273</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1304685/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006349504737376$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,3536,27903,27904,53769,53771,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15454461$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nishida, Shinpei</creatorcontrib><creatorcontrib>Nada, Tomokazu</creatorcontrib><creatorcontrib>Terazima, Masahide</creatorcontrib><title>Kinetics of Intermolecular Interaction during Protein Folding of Reduced Cytochrome c</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>Kinetics of intermolecular interaction between reduced cytochrome
c (Cyt
c) protein and solvent during the protein-refolding process is studied by monitoring the time dependence of apparent diffusion coefficient (
D) using the pulsed-laser-induced transient grating technique. The refolding was triggered by photoinduced reduction of unfolded Fe(III) Cyt
c in 3.5
M guanidine hydrochloride (GdnHCl) solution and the change in the diffusion coefficient was monitored in time domain. The relationship between
D and the protein conformations under equilibrium condition were investigated at various GdnHCl concentrations using a photolabeling reagent. The time dependence of the observed transient grating signal was analyzed using these data and two models: a continuous change model of the intermolecular interaction and a two-state model. It was found that the TG signals in various time ranges can be consistently reproduced well by the two-state model. The dynamics of
D is expressed well by a single exponential function with a rate constant of 22
±
7
s
−1 in a whole time range. The folding process of Cyt
c is discussed based on these observations.</description><subject>Biochemistry</subject><subject>Carbon Monoxide - chemistry</subject><subject>Computer Simulation</subject><subject>Cytochromes c - chemistry</subject><subject>Diffusion</subject><subject>Elasticity</subject><subject>Entropy</subject><subject>Enzyme Activation</subject><subject>Enzyme Stability</subject><subject>Guanidine - chemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Macromolecular Substances - chemistry</subject><subject>Models, Chemical</subject><subject>Oxidation-Reduction</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Proteins</subject><subject>Reaction kinetics</subject><subject>Solutions</subject><subject>Solvents - chemistry</subject><subject>Thermodynamics</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kU1v1DAQhi0EotvCL0BCEQduWcafSQ4goRUtFZVAiJ4tx550vcrai51U2n-PqyyfB07W2M_7emZeQl5QWFPJuje9j4ftMe_WFMQaBJOcPiIrKgWrAVr1mKwAQNVcdPKMnOe8A6BMAn1KzgokhVB0RW4_-YCTt7mKQ3UdJkz7OKKdR5OW0tjJx1C5OflwV31JcUIfqss4uoe6iL6imy26anOcot2muMfKPiNPBjNmfH46L8jt5Ydvm4_1zeer6837m9pKCVNte8pcyxsHZnBI-851XaeoaLgFQMW7hgMXjWpaQKdM33SSDUqatqOsSBt-Qd4tvoe536OzGKZkRn1Ifm_SUUfj9d8vwW_1XbzXlINQrSwGr08GKX6fMU9677PFcTQB45y1Uh1jpZ8CvvoH3MU5hTKcZlQ2FKhQBeILZFPMOeHwqxMK-iEz_TOzciH0kllRvfxziN-aU0gFeLsAWFZ57zHpbD2GsnSf0E7aRf_fD34A0oOqKA</recordid><startdate>20041001</startdate><enddate>20041001</enddate><creator>Nishida, Shinpei</creator><creator>Nada, Tomokazu</creator><creator>Terazima, Masahide</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</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>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>S0X</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20041001</creationdate><title>Kinetics of Intermolecular Interaction during Protein Folding of Reduced Cytochrome c</title><author>Nishida, Shinpei ; Nada, Tomokazu ; Terazima, Masahide</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c550t-cb12d837d0afde1b9d99961473c00e6397303476780ed6ab7952f65a8912b1273</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Biochemistry</topic><topic>Carbon Monoxide - chemistry</topic><topic>Computer Simulation</topic><topic>Cytochromes c - chemistry</topic><topic>Diffusion</topic><topic>Elasticity</topic><topic>Entropy</topic><topic>Enzyme Activation</topic><topic>Enzyme Stability</topic><topic>Guanidine - chemistry</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Macromolecular Substances - chemistry</topic><topic>Models, Chemical</topic><topic>Oxidation-Reduction</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Proteins</topic><topic>Reaction kinetics</topic><topic>Solutions</topic><topic>Solvents - chemistry</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nishida, Shinpei</creatorcontrib><creatorcontrib>Nada, Tomokazu</creatorcontrib><creatorcontrib>Terazima, Masahide</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nishida, Shinpei</au><au>Nada, Tomokazu</au><au>Terazima, Masahide</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetics of Intermolecular Interaction during Protein Folding of Reduced Cytochrome c</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2004-10-01</date><risdate>2004</risdate><volume>87</volume><issue>4</issue><spage>2663</spage><epage>2675</epage><pages>2663-2675</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>Kinetics of intermolecular interaction between reduced cytochrome
c (Cyt
c) protein and solvent during the protein-refolding process is studied by monitoring the time dependence of apparent diffusion coefficient (
D) using the pulsed-laser-induced transient grating technique. The refolding was triggered by photoinduced reduction of unfolded Fe(III) Cyt
c in 3.5
M guanidine hydrochloride (GdnHCl) solution and the change in the diffusion coefficient was monitored in time domain. The relationship between
D and the protein conformations under equilibrium condition were investigated at various GdnHCl concentrations using a photolabeling reagent. The time dependence of the observed transient grating signal was analyzed using these data and two models: a continuous change model of the intermolecular interaction and a two-state model. It was found that the TG signals in various time ranges can be consistently reproduced well by the two-state model. The dynamics of
D is expressed well by a single exponential function with a rate constant of 22
±
7
s
−1 in a whole time range. The folding process of Cyt
c is discussed based on these observations.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15454461</pmid><doi>10.1529/biophysj.104.042531</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3495 |
| ispartof | Biophysical journal, 2004-10, Vol.87 (4), p.2663-2675 |
| issn | 0006-3495 1542-0086 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1304685 |
| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Biochemistry Carbon Monoxide - chemistry Computer Simulation Cytochromes c - chemistry Diffusion Elasticity Entropy Enzyme Activation Enzyme Stability Guanidine - chemistry Hydrogen-Ion Concentration Kinetics Macromolecular Substances - chemistry Models, Chemical Oxidation-Reduction Protein Binding Protein Conformation Protein Denaturation Protein Folding Proteins Reaction kinetics Solutions Solvents - chemistry Thermodynamics |
| title | Kinetics of Intermolecular Interaction during Protein Folding of Reduced Cytochrome c |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-25T04%3A22%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Kinetics%20of%20Intermolecular%20Interaction%20during%20Protein%20Folding%20of%20Reduced%20Cytochrome%20c&rft.jtitle=Biophysical%20journal&rft.au=Nishida,%20Shinpei&rft.date=2004-10-01&rft.volume=87&rft.issue=4&rft.spage=2663&rft.epage=2675&rft.pages=2663-2675&rft.issn=0006-3495&rft.eissn=1542-0086&rft_id=info:doi/10.1529/biophysj.104.042531&rft_dat=%3Cproquest_pubme%3E724443351%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=215710146&rft_id=info:pmid/15454461&rft_els_id=S0006349504737376&rfr_iscdi=true |