Abstract
Although a β-turn consists of only four amino acids, it assumes many different types in proteins. Is this basically dependent on the tetrapeptide sequence alone or is it due to a variety of interactions with the other part of a protein? To answer this question, a residue-coupled model is proposed that can reflect the sequence-coupling effect for a tetrapeptide in not only a β-turn or non-β-turn, but also different types of a β-turn. The predicted results by the model for 6022 tetrapeptides indicate that the rates of correct prediction for β-turn types I, I′, II, II′, VI, and VIII and non-β-turns are 68.54%, 93.60%, 85.19%, 97.75%, 100%, 88.75%, and 61.02%, respectively. Each of these seven rates is significantly higher than \(\frac{1}{7}\) = 14.29%, the completely randomized rate, implying that the formation of different β-turn types or non-β-turns is considerably correlated with the sequences of a tetrapeptide.
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Chou, KC., Blinn, J.R. Classification and Prediction of β-Turn Types. J Protein Chem 16, 575–595 (1997). https://doi.org/10.1023/A:1026366706677
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DOI: https://doi.org/10.1023/A:1026366706677