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Science 23 October 1998:
Vol. 282. no. 5389, pp. 642 - 643
DOI: 10.1126/science.282.5389.642
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Perspectives

PROTEIN FOLDING:
A Glimpse of the Holy Grail?

Herman J. C. Berendsen

Every protein is folded in its "native" state. How the sequence of amino acids determines the folding conformation is an open question in biochemistry. Because of the huge number of possible foldings, computer simulation of the problem has been impossible. In his Perspective, Berendsen discusses results reported in the same issue by Duan and Kollman in which they used a computer model to simulate protein folding in a 36-residue protein. Although small, the protein contains 12,000 atoms, lending hope that computers methods may make some progress in the understanding of folding.

The author is in the Department of Biophysical Chemistry and the BIOSON Research Institute at the University of Groningen, Netherlands. E-mail: berendsen{at}chem.rug.nl

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Science. ISSN 0036-8075 (print), 1095-9203 (online)