Eugene I. Shakhnovich

TL;DR: A lattice Monte Carlo model in which the global minimum (native state) is known guarantees thermodynamic stability of the native state at a temperature where the chain does not get trapped in local minima and suggest principles for the folding of real proteins.

TL;DR: It is shown that successful folding does not require certain attributes that have been previously proposed as necessary for folding; these include a high number of short versus long-range contacts in the native state, a high content of the secondary structure in the original structure, a strong correlation between the native contact map and the interaction parameters, and the existence of aHigh number of low energy states with near-native conformation.

TL;DR: It is shown that this can be obtained by proper selection of protein sequences and a simple practical way to find these sequences is suggested.

TL;DR: The transmission coefficient for any conformation is defined to be the probability for a chain with the given conformation to fold before it unfolds, and two methods are presented by which to determine how closely any parameter of the system approximates the transmission coefficient.

TL;DR: Using a simulated annealing procedure in sequence space, sequences are designed to have sufficiently low energy in a given target conformation, which plays the role of the native structure in this study.