Capturing Invisible Motions in the Transition from Ground to Rare Excited States of T4 Lysozyme L99A.

ABSTRACT: Proteins commonly sample a number of conformational states to carry out their biological function, often requiring transitions from the ground state to higher-energy states. Characterizing the mechanisms that guide these transitions at the atomic level promises to impact our understanding of functional protein dynamics and energy landscapes. The leucine-99-to-alanine (L99A) mutant of T4 lysozyme is a model system that has an experimentally well characterized excited sparsely populated state as well as a ground state. Despite the exhaustive study of L99A protein dynamics, the conformational changes that permit transitioning to the experimentally detected excited state (∼3%, ΔG ∼2 kcal/mol) remain unclear. Here, we describe the transitions from the ground state to this sparsely populated exc

SUBMITTER: Schiffer JM 

PROVIDER: S-EPMC5071553 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature