Ubiquitin, folding kinetics

Pan, J.X., Wilson, D.J., Konermann, L. (2005) Pulsed hydrogen exchange and electrospray charge-state distribution as complementary probes of protein structure in kinetic experiments Imphcations for ubiquitin folding. Biochemistry, 44 (24), 8627-8633. 

Sivaraman, T., Arrington, C.B., Robertson, AD. (2001) Kinetics of unfolding and folding from amide hydrogen exchange in native ubiquitin. Nat Struct Biol, 8 (4), 331-333. 

Protein folding studies generally concern liquid-phase phenomena however, HDX reactions can also be conducted in the gas phase (e.g., [84-90] for an overview see [91]). For instance, multiply charged ions of several model proteins reacted with DjO in a vacuum following pseudo-first-order kinetics [85]. It was also observed that removing solvent significantly increased conformational rigidity. In other work, ions of bovine ubiquitin were... 

Ubiquitin has been the subject of a number of experimental studies as it is a small and soluble protein without disulfide linkages. The protein has a well-defined and packed hydrophobic core. There are a number of kinetic folding studies on this system, in addition to a high resolution crystal structure. 2D NMR studies of a partially unfolded form of the protein in 60% methanol indicate that approximately one-half of the molecule contains dismpted but native-like structure, while the other half is unstmctured and/or contains non-native structure. The interpretation of hydrogen-exchange experiments have led to the conclusion that this state is native-like. ... 

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