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  4. Insights into the Folding of Disulfide-Rich m-Conotoxins
 
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2018
  • Zeitschriftenaufsatz

Titel

Insights into the Folding of Disulfide-Rich m-Conotoxins

Abstract
The study of protein conformations using molecular dynamics (MD) simulations has been in place for decades. A major contribution to the structural stability and native conformation of a protein is made by the primary sequence and disulfide bonds formed during the folding process. Here, we investigated m-conotoxins GIIIA, KIIIA, PIIIA, SIIIA, and SmIIIA as model peptides possessing three disulfide bonds. Their NMR structures were used for MD simulations in a novel approach studying the conformations between the folded and the unfolded states by systematically breaking the distinct disulfide bonds and monitoring the conformational stability of the peptides. As an outcome, the use of a combination of the existing knowledge and results from the simulations to classify the studied peptides within the extreme models of disulfide folding pathways, namely the bovine pancreatic trypsin inhibitor pathway and the hirudin pathway, is demonstrated. Recommendations for the design and synthesis of cysteine-rich peptides with a reduced number of disulfide bonds conclude the study.
Author(s)
Ajay Abisheck Paul George
Heimer, Pascal
Maaß, Astrid
Hamaekers, Jan
Hofmann-Apitius, Martin
Biswas, Arijit
Imhof, Diana
Zeitschrift
ACS omega
Thumbnail Image
DOI
10.1021/acsomega.8b01465
Language
Englisch
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