Conformational preferences of amino acids in globular proteins

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Abstract
In a previous paper, an objective compilation of the secondary-structure regions in more than 50 different globular proteins was produced automatically. In the present paper, these assignments of secondary structure are analyzed to give the frequency of occurrence of the 20 naturally occurring amino acids in .alpha. helix, .beta. sheet and reverse-turn secondary structure. Nineteen of these amino acids have a weak but statistically significant preference for only 1 type of secondary structure. These preferences correlate well with the chemical structure of the particular amino acids, giving a more objective classification of the conformational properties of amino acids than available before.