Influence of pH on the structure and stability of the sweet protein MNEI
Author:
Affiliation:
1. Dipartimento di Scienze e Tecnologie; Università del Sannio; Benevento Italy
2. Dipartimento di Scienze Chimiche; Università di Napoli Federico II; Naples Italy
3. BMRZ; Goethe University Frankfurt; Germany
Funder
Fondazione CON IL SUD
European Union
Seventh Framework Programme
Bio-NMR
iNEXT
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/1873-3468.12437/fullpdf
Reference35 articles.
1. Equilibrium unfolding studies of Monellin: the double-chain variant appears to be more stable than the single-chain variant;Aghera;Biochemistry,2011
2. Kinetic studies of the folding of heterodimeric monellin: evidence for switching between alternative parallel pathways;Aghera;J Mol Biol,2012
3. The utilization of competing unfolding pathways of monellin is dictated by enthalpic barriers;Aghera;Biochemistry,2013
4. Rise of the helix from a collapsed globule during the folding of monellin;Goluguri;Biochemistry,2015
5. Continuous dissolution of structure during the unfolding of a small protein;Jha;Proc Natl Acad Sci USA,2009
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