Efficient expansion, folding, and unfolding of proteins

Erik D. Nelson, Nick V. Grishin

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


We consider a nonstatistical, computationally fast experiment to identify important topological constraints in folding small globular proteins of about 100–200 amino acids. In this experiment, proteins are expanded mechanically along a path of steepest increase in the free space around residues. The pathways are often consistent with folding scenarios reported in kinetics experiments and most accurately describe obligatory or mechanic folding proteins. The results suggest that certain topological “defects” in proteins lead to preferred, entropically favorable channels down their free energy landscapes.

Original languageEnglish (US)
Pages (from-to)7
Number of pages1
JournalPhysical Review E - Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topics
Issue number5
StatePublished - 2004

ASJC Scopus subject areas

  • Statistical and Nonlinear Physics
  • Statistics and Probability
  • Condensed Matter Physics


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