Conformational and Structural Characterization of Knotted Proteins.

ABSTRACT: Knotted proteins are fascinating natural biomolecules whose backbones entangle themselves in a knot. Their particular knotted configurations provide them with a wide range of topological features. However, their folding/unfolding mechanisms, stability, and function are poorly understood. In the present work, native trapped ion mobility spectrometry-mass spectrometry (TIMS-MS) was used for characterizing structural features of two model knotted proteins: a Gordian 5₂ knot ubiquitin C-terminal hydrolase (UCH) and a Stevedore 6₁ knot (α-haloacid dehalogenase, DehI). Experimental results showed structural transitions of UCH and DehI as a function of solution composition (0-50% MeOH) and temperature (T ∼20-95 °C). An increase in the protein charge states and collisi

SUBMITTER: Jeanne Dit Fouque K 

PROVIDER: S-EPMC11790308 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature