Initial Disulfide Formation Steps in the Folding of an ω-Conotoxin
To determine whether the native disulfides of ω-conotoxins are preferentially stabilized early in the folding of these small proteins, the rates and equilibria for disulfide formation were measured for three analogues of ω-conotoxin MVIIA. In each analogue, one of the three pairs of disulfide-bonded...
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Published in | Biochemistry (Easton) Vol. 41; no. 10; pp. 3507 - 3519 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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American Chemical Society
12.03.2002
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Abstract | To determine whether the native disulfides of ω-conotoxins are preferentially stabilized early in the folding of these small proteins, the rates and equilibria for disulfide formation were measured for three analogues of ω-conotoxin MVIIA. In each analogue, one of the three pairs of disulfide-bonded Cys residues was replaced with Ala residues, leaving four Cys residues that can form six intermediates with one disulfide and three species with two disulfides. For each analogue, all of the disulfide-bonded species were identified, and the equilibrium constants for forming the individual species via exchange with oxidized and reduced glutathione were measured. These equilibrium constants represent effective concentrations of the Cys thiols and ranged from 0.01 to 0.4 M in the fully reduced protein. There was little or no preference for forming the native disulfides, and the equilibria for forming the first and second disulfides decreased only slightly upon the addition of 8 M urea. The data for the four-Cys analogues, together with equilibrium data for the six-Cys form, were also used to estimate effective concentrations for forming a third disulfide once two native disulfides are present. These effective concentrations were approximately 100 and 10 M in the presence of 0 and 8 M urea, respectively. The results indicate that there is little or no preferential formation of native interactions in the folding of these molecules until two disulfides have formed, after which there is a high degree of cooperativity among the native interactions. |
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AbstractList | To determine whether the native disulfides of omega -conotoxins are preferentially stabilized early in the folding of these small proteins, the rates and equilibria for disulfide formation were measured for three analogues of omega -conotoxin MVIIA. In each analogue, one of the three pairs of disulfide-bonded Cys residues was replaced with Ala residues, leaving four Cys residues that can form six intermediates with one disulfide and three species with two disulfides. For each analogue, all of the disulfide-bonded species were identified, and the equilibrium constants for forming the individual species via exchange with oxidized and reduced glutathione were measured. These equilibrium constants represent effective concentrations of the Cys thiols and ranged from 0.01 to 0.4 M in the fully reduced protein. There was little or no preference for forming the native disulfides, and the equilibria for forming the first and second disulfides decreased only slightly upon the addition of 8 M urea. The data for the four-Cys analogues, together with equilibrium data for the six-Cys form, were also used to estimate effective concentrations for forming a third disulfide once two native disulfides are present. These effective concentrations were approximately 100 and 10 M in the presence of 0 and 8 M urea, respectively. The results indicate that there is little or no preferential formation of native interactions in the folding of these molecules until two disulfides have formed, after which there is a high degree of cooperativity among the native interactions. To determine whether the native disulfides of ω-conotoxins are preferentially stabilized early in the folding of these small proteins, the rates and equilibria for disulfide formation were measured for three analogues of ω-conotoxin MVIIA. In each analogue, one of the three pairs of disulfide-bonded Cys residues was replaced with Ala residues, leaving four Cys residues that can form six intermediates with one disulfide and three species with two disulfides. For each analogue, all of the disulfide-bonded species were identified, and the equilibrium constants for forming the individual species via exchange with oxidized and reduced glutathione were measured. These equilibrium constants represent effective concentrations of the Cys thiols and ranged from 0.01 to 0.4 M in the fully reduced protein. There was little or no preference for forming the native disulfides, and the equilibria for forming the first and second disulfides decreased only slightly upon the addition of 8 M urea. The data for the four-Cys analogues, together with equilibrium data for the six-Cys form, were also used to estimate effective concentrations for forming a third disulfide once two native disulfides are present. These effective concentrations were approximately 100 and 10 M in the presence of 0 and 8 M urea, respectively. The results indicate that there is little or no preferential formation of native interactions in the folding of these molecules until two disulfides have formed, after which there is a high degree of cooperativity among the native interactions. |
Author | Bulaj, Grzegorz Price-Carter, Marian Goldenberg, David P |
Author_xml | – sequence: 1 givenname: Marian surname: Price-Carter fullname: Price-Carter, Marian – sequence: 2 givenname: Grzegorz surname: Bulaj fullname: Bulaj, Grzegorz – sequence: 3 givenname: David P surname: Goldenberg fullname: Goldenberg, David P |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/11876659$$D View this record in MEDLINE/PubMed |
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Cites_doi | 10.1016/S0167-4838(99)00165-X 10.1006/jmbi.1996.0576 10.1016/0022-2836(84)90077-9 10.1002/bip.360220110 10.1016/S0021-9258(19)50691-3 10.1242/jcs.108.1.287 10.1021/ja00526a042 10.1006/jmbi.1993.1437 10.1016/S0021-9258(18)54531-2 10.1146/annurev.biophys.30.1.361 10.1107/S0021889891004399 10.1006/jmbi.1995.0205 10.1146/annurev.bi.63.070194.004135 10.1002/jcb.240290406 10.1021/ja01601a025 10.1146/annurev.pa.35.040195.003423 10.1038/35011000 10.1006/jmbi.1998.1645 |
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Notes | Supported by NSF Grant MCB-9316065 and NIH Grant GM42594. Peptide synthesis and mass spectroscopy services were supported by National Cancer Institute Grant 5 P30 CA 42014 and the Huntsman Cancer Institute. M.P-C. was the recipient of a postdoctoral fellowship from the Markey Center for Protein Biophysics at the University of Utah. istex:85F49414775511E3F12A4E679EEFA7B34A04E57F ark:/67375/TPS-7BSN7KCL-B ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
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Snippet | To determine whether the native disulfides of ω-conotoxins are preferentially stabilized early in the folding of these small proteins, the rates and equilibria... To determine whether the native disulfides of omega-conotoxins are preferentially stabilized early in the folding of these small proteins, the rates and... To determine whether the native disulfides of omega -conotoxins are preferentially stabilized early in the folding of these small proteins, the rates and... |
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SubjectTerms | Amino Acid Sequence Conus Cysteine - chemistry Disulfides - metabolism Kinetics Marine Molecular Sequence Data omega -Conotoxin omega-Conotoxins - chemistry omega-Conotoxins - metabolism Peptide Mapping Protein Folding |
Title | Initial Disulfide Formation Steps in the Folding of an ω-Conotoxin |
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