Targeting the protein folding transition state by mutation: Large scale (un)folding rate accelerations without altering native stability.

Abstract excerpt

Proteins are constantly undergoing folding and unfolding transitions, with rates that determine their homeostasis in vivo and modulate their biological function. The ability to optimize these rates without affecting overall native stability is hence highly desirable for protein engineering and design. The great challenge is, however, that mutations generally affect folding and unfolding rates with inversely...

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