Identification of Folding Intermediates of Streblin, The Most Stable Serine Protease: Biophysical Analysis
Streblin, a serine proteinase from plant Streblus asper, has been used to investigate the conformational changes induced by pH, temperature, and chaotropes. The near/far UV circular dichroism activities under fluorescence emission spectroscopy and 8-aniline-1-naphthalene sulfonate (ANS) binding have...
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| Veröffentlicht in: | Applied biochemistry and biotechnology 2014-01, Vol.172 (2), p.658-671 |
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| creator | Kumar, Reetesh Tripathi, Pinki de Moraes, Fabio Rogerio Caruso, Ícaro P Jagannadham, Medicherla V |
| description | Streblin, a serine proteinase from plant Streblus asper, has been used to investigate the conformational changes induced by pH, temperature, and chaotropes. The near/far UV circular dichroism activities under fluorescence emission spectroscopy and 8-aniline-1-naphthalene sulfonate (ANS) binding have been carried out to understand the unfolding of the protein in the presence of denaturants. Spectroscopic studies reveal that streblin belongs to the α+β class of proteins and exhibits stability towards chemical denaturants, guanidine hydrochloride (GuHCl). The pH-induced transition of this protein is noncooperative for transition phases between pH 0.5 and 2.5 (midpoint, 1.5) and pH 2.5 and 10.0 (midpoint, 6.5). At pH 1.0 or lower, the protein unfolds to form acid-unfolded state, and for pH 7.5 and above, protein turns into an alkaline denatured state characterized by the absence of ANS binding. At pH 2.0 (1 M GuHCl), streblin exists in a partially unfolded state with characteristics of a molten globule state. The protein is found to exhibit strong and predominant ANS binding. In total, six different intermediate states has been identified to show protein folding pathways. |
| doi_str_mv | 10.1007/s12010-013-0565-8 |
| format | Article |
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The near/far UV circular dichroism activities under fluorescence emission spectroscopy and 8-aniline-1-naphthalene sulfonate (ANS) binding have been carried out to understand the unfolding of the protein in the presence of denaturants. Spectroscopic studies reveal that streblin belongs to the α+β class of proteins and exhibits stability towards chemical denaturants, guanidine hydrochloride (GuHCl). The pH-induced transition of this protein is noncooperative for transition phases between pH 0.5 and 2.5 (midpoint, 1.5) and pH 2.5 and 10.0 (midpoint, 6.5). At pH 1.0 or lower, the protein unfolds to form acid-unfolded state, and for pH 7.5 and above, protein turns into an alkaline denatured state characterized by the absence of ANS binding. At pH 2.0 (1 M GuHCl), streblin exists in a partially unfolded state with characteristics of a molten globule state. The protein is found to exhibit strong and predominant ANS binding. In total, six different intermediate states has been identified to show protein folding pathways.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-013-0565-8</identifier><identifier>PMID: 24108566</identifier><identifier>CODEN: ABIBDL</identifier><language>eng</language><publisher>Boston: Springer-Verlag</publisher><subject>Biochemistry ; Biological and medical sciences ; Biophysical Phenomena ; Biophysical Phenomena - drug effects ; Biophysics ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Circular Dichroism ; drug effects ; Emission spectroscopy ; Enzyme Stability ; Enzyme Stability - drug effects ; Flowers & plants ; fluorescence emission spectroscopy ; Fundamental and applied biological sciences. Psychology ; Guanidine ; Guanidine - pharmacology ; Hydrogen-Ion Concentration ; metabolism ; Naphthalene ; pharmacology ; Proteases ; Protein Denaturation ; Protein Denaturation - drug effects ; Protein folding ; Protein Folding - drug effects ; proteins ; Serine Proteases ; Serine Proteases - chemistry ; Serine Proteases - metabolism ; serine proteinases ; Spectrometry, Fluorescence ; Spectrophotometry, Ultraviolet ; Streblus ; Streblus asper ; temperature ; Thermodynamics</subject><ispartof>Applied biochemistry and biotechnology, 2014-01, Vol.172 (2), p.658-671</ispartof><rights>The Author(s) 2013</rights><rights>2015 INIST-CNRS</rights><rights>Springer Science+Business Media New York 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c590t-c500985302d0145e044f080b525f18b6e9be2c4b29b37a7fb619582f672d07943</citedby><cites>FETCH-LOGICAL-c590t-c500985302d0145e044f080b525f18b6e9be2c4b29b37a7fb619582f672d07943</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12010-013-0565-8$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-013-0565-8$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28562429$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24108566$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kumar, Reetesh</creatorcontrib><creatorcontrib>Tripathi, Pinki</creatorcontrib><creatorcontrib>de Moraes, Fabio Rogerio</creatorcontrib><creatorcontrib>Caruso, Ícaro P</creatorcontrib><creatorcontrib>Jagannadham, Medicherla V</creatorcontrib><title>Identification of Folding Intermediates of Streblin, The Most Stable Serine Protease: Biophysical Analysis</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>Streblin, a serine proteinase from plant Streblus asper, has been used to investigate the conformational changes induced by pH, temperature, and chaotropes. The near/far UV circular dichroism activities under fluorescence emission spectroscopy and 8-aniline-1-naphthalene sulfonate (ANS) binding have been carried out to understand the unfolding of the protein in the presence of denaturants. Spectroscopic studies reveal that streblin belongs to the α+β class of proteins and exhibits stability towards chemical denaturants, guanidine hydrochloride (GuHCl). The pH-induced transition of this protein is noncooperative for transition phases between pH 0.5 and 2.5 (midpoint, 1.5) and pH 2.5 and 10.0 (midpoint, 6.5). At pH 1.0 or lower, the protein unfolds to form acid-unfolded state, and for pH 7.5 and above, protein turns into an alkaline denatured state characterized by the absence of ANS binding. At pH 2.0 (1 M GuHCl), streblin exists in a partially unfolded state with characteristics of a molten globule state. The protein is found to exhibit strong and predominant ANS binding. In total, six different intermediate states has been identified to show protein folding pathways.</description><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biophysical Phenomena</subject><subject>Biophysical Phenomena - drug effects</subject><subject>Biophysics</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Circular Dichroism</subject><subject>drug effects</subject><subject>Emission spectroscopy</subject><subject>Enzyme Stability</subject><subject>Enzyme Stability - drug effects</subject><subject>Flowers & plants</subject><subject>fluorescence emission spectroscopy</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Guanidine</subject><subject>Guanidine - pharmacology</subject><subject>Hydrogen-Ion Concentration</subject><subject>metabolism</subject><subject>Naphthalene</subject><subject>pharmacology</subject><subject>Proteases</subject><subject>Protein Denaturation</subject><subject>Protein Denaturation - drug effects</subject><subject>Protein folding</subject><subject>Protein Folding - drug effects</subject><subject>proteins</subject><subject>Serine Proteases</subject><subject>Serine Proteases - chemistry</subject><subject>Serine Proteases - metabolism</subject><subject>serine proteinases</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Streblus</subject><subject>Streblus asper</subject><subject>temperature</subject><subject>Thermodynamics</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqNkk1vEzEQhlcIREPhB3CBlRAShy6Mv9Y2B6RSUYhUBFLas-Xd2ImjjR3sDVL_PROSlsIBuNiW55nXM-O3qp4SeE0A5JtCKBBogLAGRCsada-aECF0A1ST-9UEqGQNpUofVY9KWQEQqoR8WB1RTkCJtp1Uq-ncxTH40NsxpFgnX5-nYR7iop7G0eW1mwc7urILzMbsuiHEk_py6erPqYx4ZbvB1TOXQ3T115xGZ4t7W78PabO8Lqg61KfRDngsj6sH3g7FPTnsx9XV-YfLs0_NxZeP07PTi6YXGkZcAbQSDOgcCBcOOPegoBNUeKK61unO0Z53VHdMWum7lmihqG8lJkjN2XH1bq-72XZYfo_9ZTuYTQ5rm69NssH8HolhaRbpu2GaKKZ2Aq8OAjl927oymnUovRsGG13aFkMEzk8QRtl_oCAY14K3_0a51tgvZxLRF3-gq7TNOEakpAROJfwsk-ypPqdSsvO3LRIwO3-YvT8M-sPs_GEU5jy7O5vbjBtDIPDyANiCn-ezjX0ovziEKKcaObrnCobiwuU7Jf7l9ef7JG-TsYuMwlczhDgACCpbwX4A417aBg</recordid><startdate>20140101</startdate><enddate>20140101</enddate><creator>Kumar, Reetesh</creator><creator>Tripathi, Pinki</creator><creator>de Moraes, Fabio Rogerio</creator><creator>Caruso, Ícaro P</creator><creator>Jagannadham, Medicherla V</creator><general>Springer-Verlag</general><general>Springer US</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>C6C</scope><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>3V.</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><scope>7QO</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20140101</creationdate><title>Identification of Folding Intermediates of Streblin, The Most Stable Serine Protease: Biophysical Analysis</title><author>Kumar, Reetesh ; Tripathi, Pinki ; de Moraes, Fabio Rogerio ; Caruso, Ícaro P ; Jagannadham, Medicherla V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c590t-c500985302d0145e044f080b525f18b6e9be2c4b29b37a7fb619582f672d07943</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biophysical Phenomena</topic><topic>Biophysical Phenomena - drug effects</topic><topic>Biophysics</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Circular Dichroism</topic><topic>drug effects</topic><topic>Emission spectroscopy</topic><topic>Enzyme Stability</topic><topic>Enzyme Stability - drug effects</topic><topic>Flowers & plants</topic><topic>fluorescence emission spectroscopy</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Guanidine</topic><topic>Guanidine - pharmacology</topic><topic>Hydrogen-Ion Concentration</topic><topic>metabolism</topic><topic>Naphthalene</topic><topic>pharmacology</topic><topic>Proteases</topic><topic>Protein Denaturation</topic><topic>Protein Denaturation - drug effects</topic><topic>Protein folding</topic><topic>Protein Folding - drug effects</topic><topic>proteins</topic><topic>Serine Proteases</topic><topic>Serine Proteases - chemistry</topic><topic>Serine Proteases - metabolism</topic><topic>serine proteinases</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Streblus</topic><topic>Streblus asper</topic><topic>temperature</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kumar, Reetesh</creatorcontrib><creatorcontrib>Tripathi, Pinki</creatorcontrib><creatorcontrib>de Moraes, Fabio Rogerio</creatorcontrib><creatorcontrib>Caruso, Ícaro P</creatorcontrib><creatorcontrib>Jagannadham, Medicherla V</creatorcontrib><collection>AGRIS</collection><collection>Springer Nature OA Free Journals</collection><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>ProQuest Central (Corporate)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</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>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech 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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</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>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</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 Basic</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kumar, Reetesh</au><au>Tripathi, Pinki</au><au>de Moraes, Fabio Rogerio</au><au>Caruso, Ícaro P</au><au>Jagannadham, Medicherla V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of Folding Intermediates of Streblin, The Most Stable Serine Protease: Biophysical Analysis</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2014-01-01</date><risdate>2014</risdate><volume>172</volume><issue>2</issue><spage>658</spage><epage>671</epage><pages>658-671</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><coden>ABIBDL</coden><abstract>Streblin, a serine proteinase from plant Streblus asper, has been used to investigate the conformational changes induced by pH, temperature, and chaotropes. The near/far UV circular dichroism activities under fluorescence emission spectroscopy and 8-aniline-1-naphthalene sulfonate (ANS) binding have been carried out to understand the unfolding of the protein in the presence of denaturants. Spectroscopic studies reveal that streblin belongs to the α+β class of proteins and exhibits stability towards chemical denaturants, guanidine hydrochloride (GuHCl). The pH-induced transition of this protein is noncooperative for transition phases between pH 0.5 and 2.5 (midpoint, 1.5) and pH 2.5 and 10.0 (midpoint, 6.5). At pH 1.0 or lower, the protein unfolds to form acid-unfolded state, and for pH 7.5 and above, protein turns into an alkaline denatured state characterized by the absence of ANS binding. At pH 2.0 (1 M GuHCl), streblin exists in a partially unfolded state with characteristics of a molten globule state. The protein is found to exhibit strong and predominant ANS binding. In total, six different intermediate states has been identified to show protein folding pathways.</abstract><cop>Boston</cop><pub>Springer-Verlag</pub><pmid>24108566</pmid><doi>10.1007/s12010-013-0565-8</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Biochemistry Biological and medical sciences Biophysical Phenomena Biophysical Phenomena - drug effects Biophysics Biotechnology Chemistry Chemistry and Materials Science Circular Dichroism drug effects Emission spectroscopy Enzyme Stability Enzyme Stability - drug effects Flowers & plants fluorescence emission spectroscopy Fundamental and applied biological sciences. Psychology Guanidine Guanidine - pharmacology Hydrogen-Ion Concentration metabolism Naphthalene pharmacology Proteases Protein Denaturation Protein Denaturation - drug effects Protein folding Protein Folding - drug effects proteins Serine Proteases Serine Proteases - chemistry Serine Proteases - metabolism serine proteinases Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Streblus Streblus asper temperature Thermodynamics |
| title | Identification of Folding Intermediates of Streblin, The Most Stable Serine Protease: Biophysical Analysis |
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