Functional and cooperative stabilization of a two-metal (Ca, Zn) center in α-amylase derived from Flavobacteriaceae species
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Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-017-18085-4.pdf
Reference36 articles.
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3. Sammond, D. W. et al. Comparing residue clusters from thermophilic and mesophilic enzymes reveals adaptive mechanisms. PLoS ONE 11, e0145848 (2016).
4. Chen, J. & Stites, W. E. Replacement of staphylococcal nuclease hydrophobic core residues with those from thermophilic homologs indicates packing is improved in some thermostable proteins. J. Mol. Biol. 344, 271–280 (2004).
5. Gromiha, M. M., Pathak, M. C., Saraboji, K., Ortlund, E. A. & Gaucher, E. A. Hydrophobic environment is a key factor for the stability of thermophilic proteins. Proteins 81, 715–721 (2013).
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