Influence of pH on the structure and stability of the sweet protein MNEI

MNEI is a single‐chain derivative of the sweet protein monellin that, in recent years, has become an accepted model for studying protein dynamic properties such as folding and aggregation. Although MNEI is very resistant at acidic pH, exposure to neutral or alkaline pH strongly affects its stability...

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Bibliographic Details
Published in:FEBS letters 2016-10, Vol.590 (20), p.3681-3689
Main Authors: Spadaccini, Roberta, Leone, Serena, Rega, Michele Fortunato, Richter, Christian, Picone, Delia
Format: Article
Language:English
Subjects:
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy - methods
MNEI
Models, Molecular
NMR relaxation
NMR titration
Plant Proteins - chemistry
protein dynamics
Protein Folding
Protein Stability
Protein Structure, Secondary
Temperature
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Summary:MNEI is a single‐chain derivative of the sweet protein monellin that, in recent years, has become an accepted model for studying protein dynamic properties such as folding and aggregation. Although MNEI is very resistant at acidic pH, exposure to neutral or alkaline pH strongly affects its stability. We have performed a thorough NMR study of the dynamic properties of MNEI at different pHs. The results demonstrate that, at physiological temperature, exposure to higher pH increases MNEI flexibility. The changes, originating from a well‐defined region in the protein, are transmitted to the whole structure and are likely to be the key for triggering unfolding processes.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.12437