Protein design under competing conditions for the availability of amino acids.

ABSTRACT: Isolating the properties of proteins that allow them to convert sequence into the structure is a long-lasting biophysical problem. In particular, studies focused extensively on the effect of a reduced alphabet size on the folding properties. However, the natural alphabet is a compromise between versatility and optimisation of the available resources. Here, for the first time, we include the impact of the relative availability of the amino acids to extract from the 20 letters the core necessary for protein stability. We present a computational protein design scheme that involves the competition for resources between a protein and a potential interaction partner that, additionally, gives us the chance to investigate the effect of the reduced alphabet on protein-protein interactions. We devis

SUBMITTER: Nerattini F 

PROVIDER: S-EPMC7021711 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature