A Second Look at Mini-Protein Stability: Analysis of FSD-1 Using Circular Dichroism, Differential Scanning Calorimetry, and Simulations
Mini-proteins that contain
Gespeichert in:
| Veröffentlicht in: | Biophysical journal 2009-11, Vol.97 (10), p.2803-2810 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2810 |
|---|---|
| container_issue | 10 |
| container_start_page | 2803 |
| container_title | Biophysical journal |
| container_volume | 97 |
| creator | Feng, Jianwen A. Kao, Jeff Marshall, Garland R. |
| description | Mini-proteins that contain |
| doi_str_mv | 10.1016/j.bpj.2009.08.046 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2776296</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006349509014398</els_id><sourcerecordid>1907739161</sourcerecordid><originalsourceid>FETCH-LOGICAL-c510t-8f04c883135c5bc7a25e8b3b1effbadcc1b5484bc99cb6635e2d948a103640893</originalsourceid><addsrcrecordid>eNp9ks1uEzEUhS0EomngAdggiw0sOuHe8c_MgIQUpRSQgkAKXVsej6d1mNjBnlTKE_S1cUnE36IrW_J3js-9OoQ8Q5ghoHy9nrXb9awEaGZQz4DLB2SCgpcFQC0fkgkAyILxRpyQ05TWAFgKwMfkBJsGq5KJCbmd05U1wXd0GcJ3qkf62XlXfI1htM7T1ahbN7hx_4bOvR72ySUaenqxOi-QXibnr-jCRbMbdKTnzlzH4NLmLF_73kbrR6cHujLa-1-kHkJ0GzvG_RnV-cuV22Tl6IJPT8ijXg_JPj2eU3J58f7b4mOx_PLh02K-LIxAGIu6B27qmiETRrSm0qWwdctatH3f6s4YbAWveWuaxrRSMmHLruG1RmCSQ92wKXl38N3u2o3tTM4Y9aC2OZeOexW0U_--eHetrsKNKqtKlo3MBi-PBjH82Nk0qo1Lxg6D9jbskqoYR15CTjglr-4lUVbIOEOsMvriP3QddjEvPKkShWyqCliG8ACZGFKKtv-dGkHd9UGtVe6DuuuDglrlPmTN87_H_aM4FiADbw-AzUu_cTaqZJz1xnYuWjOqLrh77H8CYS7Gjw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>215697703</pqid></control><display><type>article</type><title>A Second Look at Mini-Protein Stability: Analysis of FSD-1 Using Circular Dichroism, Differential Scanning Calorimetry, and Simulations</title><source>MEDLINE</source><source>Cell Press Free Archives</source><source>ScienceDirect Journals (5 years ago - present)</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>Feng, Jianwen A. ; Kao, Jeff ; Marshall, Garland R.</creator><creatorcontrib>Feng, Jianwen A. ; Kao, Jeff ; Marshall, Garland R.</creatorcontrib><description>Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations possible. However, not all mini-proteins are created equal. The stability and structure of FSD-1, a 28-residue mini-protein that adopted the ββα zinc-finger motif independent of zinc binding, was investigated using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The broad melting transition of FSD-1, similar to that of a helix-to-coil transition, was observed by using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The N-terminal β-hairpin was found to be flexible. The FSD-1 apparent melting temperature of 41°C may be a reflection of the melting of its α-helical segment instead of the entire protein. Thus, despite its attractiveness due to small size and purposefully designed helix, sheet, and turn structures, the status of FSD-1 as a model system for studying protein folding should be reconsidered.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/j.bpj.2009.08.046</identifier><identifier>PMID: 19917235</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino acids ; Calorimetry, Differential Scanning ; Circular Dichroism ; Computer Simulation ; Dichroism ; Differential scanning calorimetry ; DNA-Binding Proteins - chemistry ; Folding ; Hydrogen Bonding ; Melting ; Models, Chemical ; Models, Molecular ; Molecular dynamics ; Molecular structure ; Phase Transition ; Protein ; Protein Folding ; Protein Stability ; Protein Structure, Secondary ; Proteins ; Simulation ; Stability ; Temperature ; Transcription Factors - chemistry ; Transition Temperature ; Zinc</subject><ispartof>Biophysical journal, 2009-11, Vol.97 (10), p.2803-2810</ispartof><rights>2009 Biophysical Society</rights><rights>Copyright Biophysical Society Nov 15, 2009</rights><rights>2009 by the Biophysical Society.. 2009 Biophysical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c510t-8f04c883135c5bc7a25e8b3b1effbadcc1b5484bc99cb6635e2d948a103640893</citedby><cites>FETCH-LOGICAL-c510t-8f04c883135c5bc7a25e8b3b1effbadcc1b5484bc99cb6635e2d948a103640893</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/PMC2776296/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bpj.2009.08.046$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3550,27924,27925,45995,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19917235$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Feng, Jianwen A.</creatorcontrib><creatorcontrib>Kao, Jeff</creatorcontrib><creatorcontrib>Marshall, Garland R.</creatorcontrib><title>A Second Look at Mini-Protein Stability: Analysis of FSD-1 Using Circular Dichroism, Differential Scanning Calorimetry, and Simulations</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations possible. However, not all mini-proteins are created equal. The stability and structure of FSD-1, a 28-residue mini-protein that adopted the ββα zinc-finger motif independent of zinc binding, was investigated using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The broad melting transition of FSD-1, similar to that of a helix-to-coil transition, was observed by using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The N-terminal β-hairpin was found to be flexible. The FSD-1 apparent melting temperature of 41°C may be a reflection of the melting of its α-helical segment instead of the entire protein. Thus, despite its attractiveness due to small size and purposefully designed helix, sheet, and turn structures, the status of FSD-1 as a model system for studying protein folding should be reconsidered.</description><subject>Amino acids</subject><subject>Calorimetry, Differential Scanning</subject><subject>Circular Dichroism</subject><subject>Computer Simulation</subject><subject>Dichroism</subject><subject>Differential scanning calorimetry</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>Folding</subject><subject>Hydrogen Bonding</subject><subject>Melting</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Molecular dynamics</subject><subject>Molecular structure</subject><subject>Phase Transition</subject><subject>Protein</subject><subject>Protein Folding</subject><subject>Protein Stability</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Simulation</subject><subject>Stability</subject><subject>Temperature</subject><subject>Transcription Factors - chemistry</subject><subject>Transition Temperature</subject><subject>Zinc</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9ks1uEzEUhS0EomngAdggiw0sOuHe8c_MgIQUpRSQgkAKXVsej6d1mNjBnlTKE_S1cUnE36IrW_J3js-9OoQ8Q5ghoHy9nrXb9awEaGZQz4DLB2SCgpcFQC0fkgkAyILxRpyQ05TWAFgKwMfkBJsGq5KJCbmd05U1wXd0GcJ3qkf62XlXfI1htM7T1ahbN7hx_4bOvR72ySUaenqxOi-QXibnr-jCRbMbdKTnzlzH4NLmLF_73kbrR6cHujLa-1-kHkJ0GzvG_RnV-cuV22Tl6IJPT8ijXg_JPj2eU3J58f7b4mOx_PLh02K-LIxAGIu6B27qmiETRrSm0qWwdctatH3f6s4YbAWveWuaxrRSMmHLruG1RmCSQ92wKXl38N3u2o3tTM4Y9aC2OZeOexW0U_--eHetrsKNKqtKlo3MBi-PBjH82Nk0qo1Lxg6D9jbskqoYR15CTjglr-4lUVbIOEOsMvriP3QddjEvPKkShWyqCliG8ACZGFKKtv-dGkHd9UGtVe6DuuuDglrlPmTN87_H_aM4FiADbw-AzUu_cTaqZJz1xnYuWjOqLrh77H8CYS7Gjw</recordid><startdate>20091115</startdate><enddate>20091115</enddate><creator>Feng, Jianwen A.</creator><creator>Kao, Jeff</creator><creator>Marshall, Garland R.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><general>The 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>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>7TB</scope><scope>7U5</scope><scope>L7M</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20091115</creationdate><title>A Second Look at Mini-Protein Stability: Analysis of FSD-1 Using Circular Dichroism, Differential Scanning Calorimetry, and Simulations</title><author>Feng, Jianwen A. ; Kao, Jeff ; Marshall, Garland R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c510t-8f04c883135c5bc7a25e8b3b1effbadcc1b5484bc99cb6635e2d948a103640893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino acids</topic><topic>Calorimetry, Differential Scanning</topic><topic>Circular Dichroism</topic><topic>Computer Simulation</topic><topic>Dichroism</topic><topic>Differential scanning calorimetry</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>Folding</topic><topic>Hydrogen Bonding</topic><topic>Melting</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Molecular dynamics</topic><topic>Molecular structure</topic><topic>Phase Transition</topic><topic>Protein</topic><topic>Protein Folding</topic><topic>Protein Stability</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Simulation</topic><topic>Stability</topic><topic>Temperature</topic><topic>Transcription Factors - chemistry</topic><topic>Transition Temperature</topic><topic>Zinc</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Feng, Jianwen A.</creatorcontrib><creatorcontrib>Kao, Jeff</creatorcontrib><creatorcontrib>Marshall, Garland R.</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>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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Advanced Technologies Database with Aerospace</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>Feng, Jianwen A.</au><au>Kao, Jeff</au><au>Marshall, Garland R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Second Look at Mini-Protein Stability: Analysis of FSD-1 Using Circular Dichroism, Differential Scanning Calorimetry, and Simulations</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2009-11-15</date><risdate>2009</risdate><volume>97</volume><issue>10</issue><spage>2803</spage><epage>2810</epage><pages>2803-2810</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations possible. However, not all mini-proteins are created equal. The stability and structure of FSD-1, a 28-residue mini-protein that adopted the ββα zinc-finger motif independent of zinc binding, was investigated using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The broad melting transition of FSD-1, similar to that of a helix-to-coil transition, was observed by using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The N-terminal β-hairpin was found to be flexible. The FSD-1 apparent melting temperature of 41°C may be a reflection of the melting of its α-helical segment instead of the entire protein. Thus, despite its attractiveness due to small size and purposefully designed helix, sheet, and turn structures, the status of FSD-1 as a model system for studying protein folding should be reconsidered.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>19917235</pmid><doi>10.1016/j.bpj.2009.08.046</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3495 |
| ispartof | Biophysical journal, 2009-11, Vol.97 (10), p.2803-2810 |
| issn | 0006-3495 1542-0086 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2776296 |
| source | MEDLINE; Cell Press Free Archives; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Amino acids Calorimetry, Differential Scanning Circular Dichroism Computer Simulation Dichroism Differential scanning calorimetry DNA-Binding Proteins - chemistry Folding Hydrogen Bonding Melting Models, Chemical Models, Molecular Molecular dynamics Molecular structure Phase Transition Protein Protein Folding Protein Stability Protein Structure, Secondary Proteins Simulation Stability Temperature Transcription Factors - chemistry Transition Temperature Zinc |
| title | A Second Look at Mini-Protein Stability: Analysis of FSD-1 Using Circular Dichroism, Differential Scanning Calorimetry, and Simulations |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T14%3A33%3A03IST&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=A%20Second%20Look%20at%20Mini-Protein%20Stability:%20Analysis%20of%20FSD-1%20Using%20Circular%20Dichroism,%20Differential%20Scanning%20Calorimetry,%20and%20Simulations&rft.jtitle=Biophysical%20journal&rft.au=Feng,%20Jianwen%20A.&rft.date=2009-11-15&rft.volume=97&rft.issue=10&rft.spage=2803&rft.epage=2810&rft.pages=2803-2810&rft.issn=0006-3495&rft.eissn=1542-0086&rft_id=info:doi/10.1016/j.bpj.2009.08.046&rft_dat=%3Cproquest_pubme%3E1907739161%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=215697703&rft_id=info:pmid/19917235&rft_els_id=S0006349509014398&rfr_iscdi=true |