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Molecular BioSystems Vol -6

Molecular BioSystems Vol -5

Molecular BioSystems Vol -4

Molecular BioSystems Vol -3

Molecular BioSystems Vol -2

Interactions in the native state of monellin, which play a protective role against aggregation

Content Provider	Royal Society of Chemistry (RSC)
Author	Vendruscolo, Michele Szczepankiewicz, Olga Tartaglia, Gian Gaetano Nilsson, Hanna Thulin, Eva Cabaleiro-Lago, Celia Hunter, Gary J. Linse, Sara Hunter, Thérèse
Copyright Year	2011
Abstract	A series of recent studies have provided initial evidence about the role of specific intra-molecular interactions in maintaining proteins in their soluble state and in protecting them from aggregation. Here we show that the amino acid sequence of the protein monellin contains two aggregation-prone regions that are prevented from initiating aggregation by multiple non-covalent interactions that favor their burial within the folded state of the protein. By investigating the behavior of single-chain monellin and a series of five of its mutational variants using a variety of biochemical, biophysical and computational techniques, we found that weakening of the non-covalent interaction that stabilizes the native state of the protein leads to an enhanced aggregation propensity. The lag time for fibrillation was found to correlate with the apparent midpoint of thermal denaturation for the series of mutational variants, thus showing that a reduced thermal stability is associated with an increased aggregation tendency. We rationalize these findings by showing that the increase in the aggregation propensity upon mutation can be predicted in a quantitative manner through the increase in the exposure to solvent of the amyloidogenic regions of the sequence caused by the destabilization of the native state. Our findings, which are further discussed in terms of the structure of monellin and the perturbation by the amino acid substitutions of the contact surface between the two subdomains that compose the folded state of monellin, provide a detailed description of the specific intra-molecular interactions that prevent aggregation by stabilizing the native state of a protein.
Starting Page	521
Ending Page	532
Page Count	12
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	7
Issue Number	2
Journal	Molecular BioSystems
DOI	10.1039/c0mb00155d
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Mutation Denaturation (biochemistry) Solvent Protein
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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