Protein design and foldability

Protein Stability and Foldability-Designability Complementarity

We address the question of how evolution has possibly enhanced protein functionality by a complementary selection of sequences and structures. We show how the requirement of good func-tionality implies a two-way link between thermodynamic stability and resistance against mutations. The existence of families of structures emerges as a possible consequence of these evolution criteria. We discuss ...

Protein Foldability and Designability: General Physics and Pretty Chemistry

Making use of a simplified model for protein folding, it can be shown that conformations which are particularly stable when their energy is minimized with respect to amino acid sequence (in the sense that they display a large energy gap to the lowest structrally dissimilar conformation), aside from leading to fast folding, are highly designable (in the sense that many sequences target onto it i...

Solid-Phase Cell-Free Protein Synthesis to Improve Protein Foldability

Fast chain contraction during protein folding: "foldability" and collapse dynamics.

Theory indicates that at least some proteins will undergo a rapid and unimpeded collapse, like a disorganized hydrophobic chain, prior to folding. Yet experiments continue to find signs of an organized, or barrier-limited, collapse in even the fastest (approximately mus) folding proteins. Does the kinetic barrier represent a signature of the equilibrium "foldability" of these molecules? We have...

Insenstivity to close contacts and inability to predict protein foldability.

Mittal and coworkers recently (1) analyzed the spatial organization of folded proteins backbone and advocated an alternative hypothesis on protein folding stating that specific interactions among amino acids do not drive protein folding. The authors analyzed spatial distributions of Cα atoms for all amino acid pairs in about four thousands proteins available in PDB database and they found that ...