Ising Model Reprogramming of a Repeat Protein's Equilibrium Unfolding Pathway.

ABSTRACT: Repeat proteins are formed from units of 20-40 aa that stack together into quasi one-dimensional non-globular structures. This modular repetitive construction means that, unlike globular proteins, a repeat protein's equilibrium folding and thus thermodynamic stability can be analysed using linear Ising models. Typically, homozipper Ising models have been used. These treat the repeat protein as a series of identical interacting subunits (the repeated motifs) that couple together to form the folded protein. However, they cannot describe subunits of differing stabilities. Here we show that a more sophisticated heteropolymer Ising model can be constructed and fitted to two new helix deletion series of consensus tetratricopeptide repeat proteins (CTPRs). This analysis, showing an asymmetric spr

SUBMITTER: Millership C 

PROVIDER: S-EPMC4871810 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature