MKKWSDTEVFE

1. Circular dichroism (CD) spectroscopy, near-UV (pH: 6.5; beta, beta dimethylglutarate (buffer) 5 mM; Sso AcP (protein) 0.4 mg/mL)


2. Circular dichroism (CD) spectroscopy, far-UV (pH: 6.5; acetate (buffer); Sso AcP (protein) 0.2 mg/mL)


3. X-ray crystallography (100 K; )


4. Nuclear magnetic resonance (NMR) (pH: 5.6; D2O containing sodium phosphate (buffer) 50 mM; H2O/D2O (90/10%); NaCl 50 mM; Sso AcP (protein) 0.4 mM)


5. Dynamic light scattering (pH: 6.5; beta, beta-dimethylglutarate (buffer) 5 mM; NaCl 100 mM; Sso AcP (protein) 0.4 mg/mL)

1. Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P. "Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus." Proteins. 2006; 62(1): 64-79. PubMed: 16287076
   
   
2. Plakoutsi G, Taddei N, Stefani M, Chiti F. "Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation." J Biol Chem. 2004; 279(14): 14111-9. PubMed: 14724277