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
Hauptverfasser: Amir, Dan, Haas, Elisha
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container_title Biochemistry (Easton)
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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.
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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., &amp; Haas, E. 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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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source MEDLINE; American Chemical Society (ACS) Journals
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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