An Analytical Approach to the Protein Designability Problem

We present an analytical method for determining the designability of protein structures. We apply our method to the case of two-dimensional lattice structures, and give a systematic solution for the spectrum of any structure. Using this spectrum, the designability of a structure can be estimated. We outline a heirarchy of structures, from most to least designable, and show that this heirarchy depends on the potential that is used.Comment: 16 pages 4 figure

A New Algorithm for Protein Design

We apply a new approach to the reverse protein folding problem. Our method uses a minimization function in the design process which is different from the energy function used for folding. For a lattice model, we show that this new approach produces sequences that are likely to fold into desired structures. Our method is a significant improvement over previous attempts which used the energy function for designing sequences.Comment: 10 pages latex 2.09 no figures. Use uufiles to decod

Protein design: A perspective from simple tractable models

We review the recent progress in computational approaches to protein design which builds on advances in statistical-mechanical protein folding theory. In particular, we evaluate the degeneracy of the protein code (i.e. how many sequences fold into a given conformation) and outline a simple condition for ''designability`` in a protein model. From this point of view we discuss several popular protein models that were used for sequence design by several authors. We evaluate the strengths and weaknesses of popular approaches based on stochastic optimization in sequence space and discuss possible ways to improve them to bring them closer to experiment. We also discuss how sequence design affects folding and point out to some features of proteins that can be deigned ''in'' or designed ''out''}Comment: 12 pages three figure