The amino acid cysteine plays an important role in protein biochemistry. Besides its catalytic role in the active sites of enzymes it allows for the formation of disulfide bonds which are crucial for the function and stability of proteins. The presence of disulfide bonds also has profound influence on structural and dynamical properties of unfolded states of proteins. The formation of intramolecular loop structures limits the sampling of conformational space and consequently imposes specific structural as well as dynamical constraints onto an unstructured polypeptide chain. In this chapter, it is shown that NMR-spectroscopic studies on model proteins including lysozyme, bovine pancreatic trypsin inhibitor and the prion protein contribute valuably to the elucidation of protein folding and misfolding pathways and how these are impacted by disulfide bonds. Furthermore, NMR techniques are discussed that allow the characterization of unfolded states of proteins on an atomic level which is otherwise difficult to access by other techniques. © 2011 Springer Science+Business Media, LLC.
CITATION STYLE
Silvers, R., Schlepckow, K., Wirmer-Bartoschek, J., & Schwalbe, H. (2011). NMR-spectroscopic investigation of disulfide dynamics in unfolded states of proteins. Protein Reviews, 14, 217–256. https://doi.org/10.1007/978-1-4419-7273-6_10
Mendeley helps you to discover research relevant for your work.