Simplified lattice models have played an important role in protein structure prediction and
protein folding problems. These models can be useful for an initial approximation of the …

The structural mechanics of proteins that fold into functional shapes, polymers that
aggregate and form clusters, and organic macromolecules that bind to inorganic matter can …

We present a temperature-independent Monte Carlo method for the determination of the
density of states of lattice proteins that combines the fast ground-state search strategy of the …

Understanding the evolution of biopolymers is important to rationalise the directed and
undirected design of functional molecules. Large scale experiments or detailed …

We study the designability of all compact 3× 3× 3 and 6× 6 lattice‐protein structures using
the Miyazawa–Jernigan (MJ) matrix. The designability of a structure is the number of …

Determination of the native state of a protein from its amino acid sequence is the goal of
protein folding simulations, with potential applications in gene therapy and drug design …

Este trabalho tem como objetivo introduzir estudantes de física e áreas afins ao problema
de enovelamento de proteína. A proteína é uma macromolécula biológica de grande …

Understanding the evolution of biopolymers is a key element in rationalizing their structures
and functions. Simple exact models (SEMs) are well-positioned to address general …

We have exactly enumerated all sequences and conformations of hydrophobic-polar HP
proteins with chains of up to 19 monomers on the simple cubic lattice. For two variants of the …

We present an algorithm for the exhaustive enumeration of all monomer sequences and
conformations of short lattice proteins as described by the hydrophobic-polar (HP) model …