High polar content of long buried blocks of sequence in protein domains suggests selection against amyloidogenic non-polar sequences.

Abstract

Native protein structures achieve stability in part by burying hydrophobic side-chains. About 75% of all amino acid residues buried in protein interiors are non-polar. Buried residues are not uniformly distributed in protein sequences, but sometimes cluster as contiguous polypeptide stretches that run through the interior of protein domain structures. Such… (More)

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