Smaller and Faster: The 20-Residue Trp-Cage Protein Folds in 4 μs

Citations Over TimeTop 10% of 2002 papers

Abstract

We have used laser temperature jump spectroscopy to measure the folding speed of the 20-residue Trp-cage, the smallest polypeptide known to exhibit truly cooperative folding behavior. The observed folding time (4 mus at room temperature) makes this not only the smallest foldable protein, but also the fastest, with a folding speed that exceeds contact-order predictions and approaches anticipated diffusional "speed limits" for protein folding.

Related Papers

• → Contact order revisited: Influence of protein size on the folding rate(2003)374 cited
• → Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: application of long-range order to folding rate prediction11Edited by P. E. Wright(2001)293 cited
• → Protein Folding Kinetics: Barrier Effects in Chemical and Thermal Denaturation Experiments(2007)117 cited
• → The Molten Globule, and Two-State vs. Non-Two-State Folding of Globular Proteins(2020)36 cited
• → Two-State Folding Kinetics of Small Proteins in the Sequential Collapse Model: Dependence of the Folding Rate on Contact Order and Temperature(2003)12 cited