Document Detail


Catalytic unfolding and proteolysis of cytochrome C induced by synthetic binding agents.
MedLine Citation:
PMID:  15469279     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A class of polyanionic copper porphyrin dimers is shown to selectively increase the susceptibility of cytochrome c to proteolysis through binding-induced disruption of tertiary and secondary structure. The free energy of the protein conformation leading to proteolytic attack is stabilized by about 2.4 kcal/mol in the bound state. The proteolytic acceleration is catalytic in nature, requiring only a fraction of an equivalent of metalloporphyrin to effect complete, rapid digestion in the presence of a protease.
Authors:
Kevin Groves; Andrew J Wilson; Andrew D Hamilton
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  126     ISSN:  0002-7863     ISO Abbreviation:  J. Am. Chem. Soc.     Publication Date:  2004 Oct 
Date Detail:
Created Date:  2004-10-07     Completed Date:  2005-04-14     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  United States    
Other Details:
Languages:  eng     Pagination:  12833-42     Citation Subset:  IM    
Affiliation:
Contribution from the Department of Chemistry, Yale University, New Haven, CT 06511, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Catalysis
Circular Dichroism
Copper / chemistry
Cytochromes c / chemistry*
Electrophoresis, Polyacrylamide Gel
Metalloporphyrins / chemistry*
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Denaturation
Protein Folding
Protein Structure, Secondary
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spectrophotometry, Ultraviolet
Trypsin / chemistry
Grant Support
ID/Acronym/Agency:
GM 35208/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Metalloporphyrins; 7440-50-8/Copper; 9007-43-6/Cytochromes c; EC 3.4.21.4/Trypsin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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