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Unveiling the Stabilization Pathway of Mutant Proteins and Its Impact on Protein Folding

Explore the interface between Im7 mutants and E7, unveiling a new protein stabilization pathway for better folding in a conducive environment. Investigate the effects on beta-lactamase activity, poor folding, and degradation, along with Spy Cradle and normal oxidation pathways. Discover a novel oxidation pathway involving Thioredoxin under various interactions.

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Unveiling the Stabilization Pathway of Mutant Proteins and Its Impact on Protein Folding

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Presentation Transcript

  1. Stabilizing Im7 mutants map to its interface with E7

  2. PenVR PenVS Stabilization of protein or Better folding environment good folding active -lactamase poor folding degradation

  3. Spy Cradle

  4. Normal pathway SH S oxidation S Substrate proteins SH S S SH SH S S DsbA O2 DsbB Ubiquinone Cytochrome oxidases New pathway SH oxidation S S SH SH S S SH Thioredoxin Thioredoxin S S S Fe Fe S S S O2 membrane cytoplasm

  5. DsbC-like Mutant DsbG-K113E Reverses Charge to resemble DsbC DsbC DsbG wt DsbG-K113E

  6. MDH interactions with HdeA-F35W W35 + MDH lmax=336 nm - MDH lmax=346 nm

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