Nucleation in conformation transitions of biological systems

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The analogy between the conformation transition in biological systems and the first-order phase transition has been widely received for understanding protein folding. Nucleation has been considered as the initial step in the folding mechanism [1, 2]. The α-helix is a basic secondary structural element of proteins. In the helix-coil transition theory, the transition is characterized by two parameters: the nucleation parameter and the propagation parameter. The nucleation parameter is in the order of 10 -5 to 10 -2, and the propagation parameter is in the order of 1, indicating that the probability of nucleation is low and the propagation is much faster. This theory predicts that helix folding is highly cooperative, in analogy to the first-order phase transition. We have carried out molecular simulations on peptide folding and compared the simulation with the theory and experimental results.

Original languageEnglish (US)
Pages (from-to)605-607
Number of pages3
JournalInorganic Materials
Issue number6
StatePublished - 1999

All Science Journal Classification (ASJC) codes

  • Chemical Engineering(all)
  • Inorganic Chemistry
  • Metals and Alloys
  • Materials Chemistry


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