Abstract
Two possibilities exist for the evolution of individual enzymes/proteins from a milieu of amino acids, one based on preference and selectivity and the other on the basis of random events. Logic is overwhelmingly in favour of the former. By protein data base analysis and experiments, we have provided data to show the manifestation of two types of preferences, namely, the choice of the neighbour and its acceptance from the amino end (left) or the carboxyl end (right). The study tends to show that if the 20 proteinous amino acids were made to combine in water, the resulting profile would be nonrandom. Such selectivity could be a factor in protein evolution.
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Dedicated to the memory of Darshan Ranganathan.
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Ranganathan, S., Kundu, D. & Vudayagiri, S.D. Protein evolution: intrinsic preferences in peptide bond formation: a computational and experimental analysis. J Biosci 28, 683–690 (2003). https://doi.org/10.1007/BF02708428
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DOI: https://doi.org/10.1007/BF02708428