Loop fold structure of proteins: resolution of Levinthas paradox - PubMed (original) (raw)

Loop fold structure of proteins: resolution of Levinthas paradox

Igor N Berezovsky et al. J Biomol Struct Dyn. 2002 Aug.

Abstract

According to Levinthal a protein chain of ordinary size would require enormous time to sort its conformational states before the final fold is reached. Experimentally observed time of folding suggests an estimate of the chain length for which the time would be sufficient. This estimate by order of magnitude fits to experimentally observed universal closed loop elements of globular proteins - 25-30 residues.

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• Back to units of protein folding.
  Berezovsky IN, Trifonov EN. Berezovsky IN, et al. J Biomol Struct Dyn. 2002 Dec;20(3):315-6. doi: 10.1080/07391102.2002.10506847. J Biomol Struct Dyn. 2002. PMID: 12437367

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