pH driven fibrillar aggregation of the super-sweet protein Y65R-MNEI: A step-by-step structural analysis-Reference-Cited by-同舟云学术

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pH driven fibrillar aggregation of the super-sweet protein Y65R-MNEI: A step-by-step structural analysis

Published:2018-04 Issue:4 Volume:1862 Page:808-815
ISSN:0304-4165
Container-title:Biochimica et Biophysica Acta (BBA) - General Subjects
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - General Subjects

Author:

Pica Andrea,Leone Serena,Di Girolamo Rocco,Donnarumma Federica,Emendato Alessandro,Rega Michele Fortunato,Merlino Antonello,Picone Delia

Funder

Fondazione con il SUD

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference55 articles.

1. Purification of monellin, the sweet principle of Dioscoreophyllum cumminsii;Morris;Biochim. Biophys. Acta Gen. Subj.,1972

2. Isolation and characterization of the sweet principle from Dioscoreophyllum cumminsii (stapf) Diels;van der Wel;FEBS Lett.,1972

3. Redesigning a sweet protein: increased stability and renaturability;Kim;Protein Eng.,1989

4. Structural determination of the active site of a sweet protein a 1H NMR investigation of pMNEI;Tancredi;FEBS Lett.,1992

5. Acetate: friend or foe? Efficient production of a sweet protein in Escherichia coli BL21 using acetate as a carbon source;Leone;Microb. Cell Factories,2015

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2. Structural insights and aggregation propensity of a super-stable monellin mutant: A new potential building block for protein-based nanostructured materials;International Journal of Biological Macromolecules;2024-01

3. Review on the applications of atomic force microscopy imaging in proteins;Micron;2022-08

4. A Super Stable Mutant of the Plant Protein Monellin Endowed with Enhanced Sweetness;Life;2021-03-12

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