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Updated: Aug 13, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
Published on: January 26, 2024
Amino acid propensities revisited
Orlando E Acevedo1, Leonardo R Lareo
1Computational and Structural Biochemistry and Bioinformatics, Department of Nutrition and Biochemistry, School of Sciences, Pontificia Universidad Javeriana, Carlos Ortiz Building, Rm. 107, Carrera 7a #43-82, Bogotá, Colombia.
Abstract:
Statistical analysis of amino acid patterns in approximately 160,000 alpha-helices in experimentally determined structures revealed di-, tri-, and tetrapeptides, whose frequencies deviate most from the statistical model. Importantly, some sequences were never found in alpha- helices. This fact was detected initially with tripeptides, where nearly 1% of the possible sequences were never seen in the helical segments. For tetrapeptides, this effect is very strong and significant; almost 43% of the possible sequences never appear in alpha-helices. It is possible that there are some steric and energetic restrictions that do not allow these tetrameric amino acid sequences to form alpha-helical structure.
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