Reduced bovine pancreatic trypsin inhibitor has a compact structure
The conformation of reduced bovine pancreatic trypsin inhibitor (R-BPTI) under reducing conditions was monitored by measurements of nonradiative excitation energy-transfer efficiencies (E) between a donor probe attached to the N-terminal Arg1 residue and an acceptor attached to one of the lysine res...
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Veröffentlicht in: | Biochemistry (Easton) 1988-12, Vol.27 (25), p.8889-8893 |
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creator | Amir, Dan Haas, Elisha |
description | The conformation of reduced bovine pancreatic trypsin inhibitor (R-BPTI) under reducing conditions was monitored by measurements of nonradiative excitation energy-transfer efficiencies (E) between a donor probe attached to the N-terminal Arg1 residue and an acceptor attached to one of the lysine residues (15, 26, 41, or 46) [Amir, D., & Haas, E. (1987) Biochemistry 26, 2162-2175]. High-excitation energy-transfer efficiencies that approach those found in the native state were obtained for the reduced labeled BPTI derivatives in 0.5 M guanidine hydrochloride (Gdn.HCl) and 4 mM DTT. Unlike the dependence expected for a random coil chain, E does not decrease as a function of the number of residues between the labeled sites. The efficiency of energy transfer between probes attached to residues 1 and 15 in the reduced state is higher than that found for the same pair of sites in the native state or reduced unfolded (in 6 M Gdn.HCl) state. This segment also shows high dynamic flexibility. These results indicate that the overall structure of reduced BPTI under folding (but still reducing) conditions shows a high population of conformers with interprobe distances similar to those of the native state. Reduced BPTI seems to be in a molten globule state characterized by a flexible, compact structure, which probably reorganizes into the native structure when the folding is allowed to proceed under oxidizing conditions. |
doi_str_mv | 10.1021/bi00425a003 |
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(1987) Biochemistry 26, 2162-2175]. High-excitation energy-transfer efficiencies that approach those found in the native state were obtained for the reduced labeled BPTI derivatives in 0.5 M guanidine hydrochloride (Gdn.HCl) and 4 mM DTT. Unlike the dependence expected for a random coil chain, E does not decrease as a function of the number of residues between the labeled sites. The efficiency of energy transfer between probes attached to residues 1 and 15 in the reduced state is higher than that found for the same pair of sites in the native state or reduced unfolded (in 6 M Gdn.HCl) state. This segment also shows high dynamic flexibility. These results indicate that the overall structure of reduced BPTI under folding (but still reducing) conditions shows a high population of conformers with interprobe distances similar to those of the native state. Reduced BPTI seems to be in a molten globule state characterized by a flexible, compact structure, which probably reorganizes into the native structure when the folding is allowed to proceed under oxidizing conditions.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00425a003</identifier><identifier>PMID: 2466482</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; Aprotinin ; Biological and medical sciences ; Disulfides ; Dithiothreitol ; Edetic Acid ; Energy Transfer ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Guanidine ; Guanidines ; Hydrolases ; Oxidation-Reduction ; Protein Conformation ; Spectrometry, Fluorescence ; Trypsin Inhibitors</subject><ispartof>Biochemistry (Easton), 1988-12, Vol.27 (25), p.8889-8893</ispartof><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a383t-2ccdc57afe724acbeb4c5974f53434137bcc6ce4f8a7992662ae77d28ed949d43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00425a003$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00425a003$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6696933$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2466482$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Amir, Dan</creatorcontrib><creatorcontrib>Haas, Elisha</creatorcontrib><title>Reduced bovine pancreatic trypsin inhibitor has a compact structure</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The conformation of reduced bovine pancreatic trypsin inhibitor (R-BPTI) under reducing conditions was monitored by measurements of nonradiative excitation energy-transfer efficiencies (E) between a donor probe attached to the N-terminal Arg1 residue and an acceptor attached to one of the lysine residues (15, 26, 41, or 46) [Amir, D., & Haas, E. (1987) Biochemistry 26, 2162-2175]. High-excitation energy-transfer efficiencies that approach those found in the native state were obtained for the reduced labeled BPTI derivatives in 0.5 M guanidine hydrochloride (Gdn.HCl) and 4 mM DTT. Unlike the dependence expected for a random coil chain, E does not decrease as a function of the number of residues between the labeled sites. The efficiency of energy transfer between probes attached to residues 1 and 15 in the reduced state is higher than that found for the same pair of sites in the native state or reduced unfolded (in 6 M Gdn.HCl) state. This segment also shows high dynamic flexibility. These results indicate that the overall structure of reduced BPTI under folding (but still reducing) conditions shows a high population of conformers with interprobe distances similar to those of the native state. Reduced BPTI seems to be in a molten globule state characterized by a flexible, compact structure, which probably reorganizes into the native structure when the folding is allowed to proceed under oxidizing conditions.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Aprotinin</subject><subject>Biological and medical sciences</subject><subject>Disulfides</subject><subject>Dithiothreitol</subject><subject>Edetic Acid</subject><subject>Energy Transfer</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Guanidine</subject><subject>Guanidines</subject><subject>Hydrolases</subject><subject>Oxidation-Reduction</subject><subject>Protein Conformation</subject><subject>Spectrometry, Fluorescence</subject><subject>Trypsin Inhibitors</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkM9P3DAQha0KBAvtiTNSDogeqlDHduz4iFYUkID-ouJoTSYTYbqbBNtB8N83q12teuA0enqfnkYfY0cFPyu4KL7WnnMlSuBcfmCzohQ8V9aWO2zGOde5sJrvs4MYn6aouFF7bE8orVUlZmz-i5oRqcnq_sV3lA3QYSBIHrMU3obou8x3j772qQ_ZI8QMMuyXA2DKYgojpjHQR7bbwiLSp809ZH--XdzPr_Kb75fX8_ObHGQlUy4QGywNtGSEAqypVlhao9pSKqkKaWpEjaTaCoy1QmsBZEwjKmqsso2Sh-x0vTuE_nmkmNzSR6TFAjrqx-hMZSYffAV-WYMY-hgDtW4IfgnhzRXcrZS5_5RN9PFmdqyX1GzZjaOpP9n0EBEWbZgU-bjFtLbaytVMvsZ8TPS6rSH8ddpIU7r7H7_dz9vLq9u7h7krJv7zmgeM7qkfQze5e_fBf9kKjxE</recordid><startdate>19881213</startdate><enddate>19881213</enddate><creator>Amir, Dan</creator><creator>Haas, Elisha</creator><general>American Chemical Society</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>19881213</creationdate><title>Reduced bovine pancreatic trypsin inhibitor has a compact structure</title><author>Amir, Dan ; Haas, Elisha</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a383t-2ccdc57afe724acbeb4c5974f53434137bcc6ce4f8a7992662ae77d28ed949d43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Aprotinin</topic><topic>Biological and medical sciences</topic><topic>Disulfides</topic><topic>Dithiothreitol</topic><topic>Edetic Acid</topic><topic>Energy Transfer</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Guanidine</topic><topic>Guanidines</topic><topic>Hydrolases</topic><topic>Oxidation-Reduction</topic><topic>Protein Conformation</topic><topic>Spectrometry, Fluorescence</topic><topic>Trypsin Inhibitors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Amir, Dan</creatorcontrib><creatorcontrib>Haas, Elisha</creatorcontrib><collection>Istex</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>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Amir, Dan</au><au>Haas, Elisha</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reduced bovine pancreatic trypsin inhibitor has a compact structure</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1988-12-13</date><risdate>1988</risdate><volume>27</volume><issue>25</issue><spage>8889</spage><epage>8893</epage><pages>8889-8893</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The conformation of reduced bovine pancreatic trypsin inhibitor (R-BPTI) under reducing conditions was monitored by measurements of nonradiative excitation energy-transfer efficiencies (E) between a donor probe attached to the N-terminal Arg1 residue and an acceptor attached to one of the lysine residues (15, 26, 41, or 46) [Amir, D., & Haas, E. (1987) Biochemistry 26, 2162-2175]. High-excitation energy-transfer efficiencies that approach those found in the native state were obtained for the reduced labeled BPTI derivatives in 0.5 M guanidine hydrochloride (Gdn.HCl) and 4 mM DTT. Unlike the dependence expected for a random coil chain, E does not decrease as a function of the number of residues between the labeled sites. The efficiency of energy transfer between probes attached to residues 1 and 15 in the reduced state is higher than that found for the same pair of sites in the native state or reduced unfolded (in 6 M Gdn.HCl) state. This segment also shows high dynamic flexibility. These results indicate that the overall structure of reduced BPTI under folding (but still reducing) conditions shows a high population of conformers with interprobe distances similar to those of the native state. Reduced BPTI seems to be in a molten globule state characterized by a flexible, compact structure, which probably reorganizes into the native structure when the folding is allowed to proceed under oxidizing conditions.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>2466482</pmid><doi>10.1021/bi00425a003</doi><tpages>5</tpages></addata></record> |
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subjects | Analytical, structural and metabolic biochemistry Aprotinin Biological and medical sciences Disulfides Dithiothreitol Edetic Acid Energy Transfer Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Guanidine Guanidines Hydrolases Oxidation-Reduction Protein Conformation Spectrometry, Fluorescence Trypsin Inhibitors |
title | Reduced bovine pancreatic trypsin inhibitor has a compact structure |
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