71 citations · 179 across the 7 of their papers we have counts for
7 papers
The looping probability of random heteropolymers helps to understand the scaling properties of biopolymers
Y. Zhan, L. Giorgetti, G. Tiana
Random heteropolymers are a minimal description of biopolymers and can provide a theoretical framework to the investigate the formation of loops in biophysical experiments. A two--…
Equilibrium properties of realistic random heteropolymers and their relevance for globular and naturally unfolded proteins
Guido Tiana, Ludovico Sutto
Random heteropolymers do not display the typical equilibrium properties of globular proteins, but are the starting point to understand the physics of proteins and, in particular, t…
Designability of lattice model heteropolymers
G. Tiana, R. A. Broglia, D. Provasi
Protein folds are highly designable, in the sense that many sequences fold to the same conformation. In the present work we derive an expression for the designability in a 20 lette…
Statistical Analysis of Native Contact Formation in the Folding of Designed Model Proteins
G. Tiana, R. A. Broglia
The time evolution of the formation probability of native bonds has been studied for designed sequences which fold fast into the native conformation. From this analysis a clear hie…
Stability of Designed Proteins Against Mutations
R. A Broglia, G. Tiana, H. E. Roman +2
The stability of model proteins with designed sequences is assessed in terms of the number of sequences (obtained from the designed sequence through mutations), which fold into 5th…
Mapping of mutation-sensitive sites in protein-like chains
M. Skorobogatiy, G. Tiana
In this work we have studied, with the help of a simple on-lattice model, the distribution pattern of sites sensitive to point mutations ('hot' sites) in protein-like chains. It ha…