Journal of Chemical Physics, vol. 112, 2050-2055 (2000)
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<b>A novel iterative strategy for protein design</b> 
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Andrea Rossi, Amos Maritan, and Cristian Micheletti
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<a href="http://dx.doi.org/10.1063/1.480766">Link to online article, </a><br>

ABSTRACT We propose and discuss a novel strategy for protein
design. The method is based on recent theoretical advancements which
showed the importance to treat carefully the conformational free
energy of designed sequences. In this work we show how computational
cost can be kept to a minimum by encompassing negative design
features, i.e., isolating a small number of structures that compete
significantly with the target one for being occupied at low
temperature. The method is successfully tested on minimalist protein
models and using a variety of amino acid interaction potentials.