Detection-dependent kinetics as a probe of folding landscape microstructure

Wei Yuan Yang, Martin Gruebele

Research output: Contribution to journalArticlepeer-review


The folding landscapes of polypeptides and proteins exhibit a hierarchy of local minima. The causes range from proline isomerization all the way down to microstructure in the free energy caused by residual frustration inherent in even the best 20 amino acid design. The corresponding time scales range from hours to submicroseconds. The smallest microstructures are difficult to detect. We have measured the folding/unfolding kinetics of the engineered trpzip2 peptide at different tryptophan fluorescence wavelengths, each yielding a different rate. Wavelength-dependent folding kinetics on 0.1-2 μs time scales show that different microstructures with a range of solvent exposure and local dynamics are populated. We estimate a lower limit for the roughness of the free energy surface based on the range of rates observed.

Original languageEnglish (US)
Pages (from-to)7758-7759
Number of pages2
JournalJournal of the American Chemical Society
Issue number25
StatePublished - Jun 30 2004

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


Dive into the research topics of 'Detection-dependent kinetics as a probe of folding landscape microstructure'. Together they form a unique fingerprint.

Cite this