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Conjecture on the Design of Helical Proteins.

John J KozakHarry B Gray
Published in: The journal of physical chemistry. B (2020)
In an important advance in our understanding of protein folding, Wolynes and Onuchic found that the frustration ratio, Tf/Ts, for funneled energy landscapes is Tf/Ts ∼1.6. In our recent work on four heme proteins, we showed that when a protein unfolds from the native state to an early unfolded state, the degree of departure is characterized by a ratio f ∼1.6, where f is a measure of the elongation of n-residue segments of the polypeptide chain. Our analysis, which accounts for this apparent similarity in calculated signatures, is based on a logistic-map model of unfolding. We offer an important take home for the de novo protein synthesis community: in order to increase the probability of obtaining good quality crystals, nearest-neighbor repulsive interactions between adjacent residues (or sequences of residues) in the polypeptide chain must be propagated correctly.
Keyphrases
  • healthcare
  • amino acid
  • protein protein
  • mental health
  • binding protein
  • genome wide
  • gene expression
  • molecular dynamics simulations
  • endoplasmic reticulum stress
  • computed tomography
  • diffusion weighted imaging