Abstract
Analysis of β-sheet sandwiches (for example immunoglobulin domains) suggests an algorithm that successfully predicts the tertiary fold of these proteins from their sequence and secondary structure. We propose tertiary structures for β2- microglobulin and an HLA-B7 antigen fragment. Topological rules are presented that markedly reduce the number of folds for proteins in which a-helices pack against a parallel β-sheet.
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Cohen, F., Sternberg, M. & Taylor, W. Analysis and prediction of protein β-sheet structures by a combinatorial approach. Nature 285, 378–382 (1980). https://doi.org/10.1038/285378a0
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DOI: https://doi.org/10.1038/285378a0
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