Proceedings of the National Academy of Sciences · 1992 · 244 citations · 33 references
Life SciencesBiochemistryBiophysicsProtein BiochemistryProtein Structure PredictionStructural BiologyAmino Acid ChemistryAmino Acid Sequence DeterminantsAmino Acid StructureProtein StructureSecondary StructureSecondary Structure FormationAlpha HelicesAmino Acid Sequence EffectsAmino Acid Sequence-structure RelationshipsComputational Prediction Of Amino Acid ConformationProtein Secondary Structure PredictionSecondary Structure PropensityX-ray Crystallography Of Amino AcidsX-ray Diffraction Analysis
Three equivocal amino acid sequences were synthesized that are predicted to be alpha-helical from amino acid preference but are found to be primarily beta-strand from x-ray diffraction of their respective proteins. In some solvent systems we recover the alpha-helical structure predicted by amino acid preference, whereas in other systems we mimic the interior of the protein and produce a beta-strand. These results are experimental proof that the environment is important in determining the secondary structure formed by an amino acid sequence; therefore schemes that predict secondary structure from amino acid sequence alone can never be totally successful.
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