Prior work has shown that small proteins can fold (i.e., convert from unstructured to structured states) within 10 μs. Here we use time-resolved solid state nuclear magnetic resonance (ssNMR) methods to show that full folding of the 35-residue villin headpiece subdomain (HP35) requires a slow annealing process that has not been previously detected. ^{13}C ssNMR spectra of frozen HP35 solutions, acquired with a variable time τ_{e} at 30 °C after rapid cooling from 95 °C and before rapid freezing, show changes on the 3-10 ms timescale, attributable to slow rearrangements of protein sidechains during τ_{e}.
Keyphrases
- solid state
- magnetic resonance
- molecular dynamics simulations
- single molecule
- amino acid
- protein protein
- multiple sclerosis
- mass spectrometry
- loop mediated isothermal amplification
- binding protein
- ms ms
- small molecule
- magnetic resonance imaging
- density functional theory
- computed tomography
- contrast enhanced
- molecular dynamics