Abstract
Abstract: A new algorithm producing a large number of divergent sequences which can adopt a defined structure is proposed. The algorithm can be applied to proteins of any size. This is achieved by constraining the amino acid composition to the native one and minimising the pseudoenergy function by "shuffling" the sequence. The algorithm is tested by sequence design for five different protein structures. Modelling by homology with the use of resultant sequences produces "proper" protein structures as judged using several different methods
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