Unfolded conformations of α-lytic protease are more stable than its native state
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/27470.pdf
Reference17 articles.
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3. Fujinaga, M., Delbaere, L. T., Brayer, G. D. & James, M. N. Refined structure of α-lytic protease at 1.7 Å resolution. Analysis of hydrogen bonding and solvent structure. J. Mol. Biol. 184, 479–502 (1985).
4. Makhatadze, G. I. & Privalov, P. L. Energetics of protein structure. Adv. Protein Chem. 47, 307–425 (1995).
5. Peters, R. J. et al. Pro region C-terminus: Protease active site interactions are critical in catalyzing the folding of α-lytic protease. Biochemistry 37, 12058–12067 (1998).
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