Unperturbed Detection of the Dynamic Structure in the Hydrophobic Core of Trp-Cage via Two-Dimensional Infrared Spectroscopy.

ABSTRACT: The tyrosine ring mode is an intrinsic non-perturbing site-specific infrared reporter for conformational dynamics within protein systems. This transition is influenced by direct and indirect interactions associated with the electron-donating ability and the hydrophobicity of the surrounding molecules. Utilizing an intrinsic tyrosine moiety, two-dimensional infrared spectra of Trp-cage, often called the "hydrogen atom" of protein folding, were measured in the folded and denatured states to uncover the dynamics of the hydrophobic core. The vibrational lifetimes and the correlation decays of the tyrosine ring mode showed significant changes upon both temperature and chemical denaturation of the Trp-cage miniprotein, indicating important structural features of the hydrophobic core and its dyna

SUBMITTER: Chalyavi F 

PROVIDER: S-EPMC7026909 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature