Single-Molecule Chemo-Mechanical Spectroscopy Provides Structural Identity of Folding Intermediates.

ABSTRACT: Single-molecule force spectroscopy has emerged as a powerful tool for studying the folding of biological macromolecules. Mechanical manipulation has revealed a wealth of mechanistic information on transient and intermediate states. To date, the majority of state assignment of intermediates has relied on empirical demarcation. However, performing such experiments in the presence of different osmolytes provides an alternative approach that reports on the structural properties of intermediates. Here, we analyze the folding and unfolding of T4 lysozyme with optical tweezers under a chemo-mechanical perturbation by adding osmolytes. We find that two unrelated protective osmolytes, sorbitol and trimethylamine-n-oxide, function by marginally decelerating unfolding rates and specifically modulatin

SUBMITTER: Motlagh HN 

PROVIDER: S-EPMC4816687 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature