Abstract
Understanding protein folding is of fundamental and practical importance in chemistry and biology. Despite the great success that has been made in tackling this problem, a detailed knowledge of how the elementary processes such as hydrogen-bond formation occur during protein folding has remained largely elusive. Using the combined power of molecular dynamics simulation with electrostatic polarization and coherent two-dimensional infrared spectroscopy, we are able to delineate the order of the hydrogen-bond formation event of a 17-residue peptide during its folding from an extended state to the native α-helix state. The folding is carried out by a single trajectory room-temperature molecular dynamics simulation that includes the polarization effect of hydrogen bonding, which is critical to the successful folding of the peptide. The onset and evolution of the isotope-labeled amide I vibration diagonal and cross peaks on the simulated 2DIR spectra allow us to build a structure-spectrum connection, and thus provide a microscopic picture of the helix folding process.
Original language | English (US) |
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Pages (from-to) | 15681-15688 |
Number of pages | 8 |
Journal | Physical Chemistry Chemical Physics |
Volume | 12 |
Issue number | 48 |
DOIs | |
State | Published - Dec 28 2010 |
ASJC Scopus subject areas
- Physics and Astronomy(all)
- Physical and Theoretical Chemistry