Structure, three-dimensional molten globule state

Staniforth, R. A., Giannini, S., Higgins, L. D., Conroy, M. J., Hounslow, A. M.,Jerala, R., Craven, C. J., and Waltho, J. P. (2001). Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J. 20, 4774-4781. 

Staniforth RA, et al. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J. 2001 20 4774-4781. 

Even more information may be obtained by the. separate determination of A// and AS from differential scanning calorimetry, from the binding of 8-anilino-l-naphthalenesul-fonic acid, a fluorescent dye which preferentially binds to the molten globule state, and from proton exchange rates determined by NMR spectroscopy. Ultimately, all of these methods are required for a complete characterization of the protein. The final test remains the determination of the three-dimensional structure by X-ray crystallography or NMR. For a soluble, stable, folded protein, this should generally be possible. 

---