Monitoring Unfolding of Titin I27 Single and Bi Domain with High-Pressure NMR Spectroscopy.

ABSTRACT: A complete description of the pathways and mechanisms of protein folding requires a detailed structural and energetic characterization of the folding energy landscape. Simulations, when corroborated by experimental data yielding global information on the folding process, can provide this level of insight. Molecular dynamics (MD) has often been combined with force spectroscopy experiments to decipher the unfolding mechanism of titin immunoglobulin-like single or multidomain, the giant multimodular protein from sarcomeres, yielding information on the sequential events during titin unfolding under stretching. Here, we used high-pressure NMR to monitor the unfolding of titin I27 Ig-like single domain and tandem. Because this method brings residue-specific information on the folding process, it

SUBMITTER: Herrada I 

PROVIDER: S-EPMC6051020 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature