Title
Effect of protein charge on the generation of aggregation-prone conformers
Author
Broersen, K.
Weijers, M.
de Groot, J.
Hamer, R.J.
de Jongh, H.H.J.
TNO Kwaliteit van Leven
Publication year
2007
Abstract
This study describes how charge modification affects aggregation of ovalbumin, thereby distinguishing the role of conformational and electrostatic stability in the process. Ovalbumin variants were engineered using chemical methylation or succinylation to obtain a range of protein net charge from -1 to -26. Charge modification significantly affected the denaturation temperature. From urea-induced equilibrium denaturation studies, it followed that unfolding proceeded via an intermediate state. However, the heat-induced denaturation process could still be described as a two-state irreversible unfolding transition, suggesting that the occurrence of an intermediate has no influence on the kinetics of unfolding. By monitoring the aggregation kinetics, the net charge was found not to be discriminative in the process. It is concluded that the dominant factor determining ovalbumin aggregation propensity is the rate of denaturation and not electrostatic repulsive forces. © 2007 American Chemical Society.
Subject
Nutrition
Food technology
Chemical modification
Conformations
Denaturation
Electrostatics
Methylation
Proteins
Temperature
Aggregation kinetics
Conformers
Electrostatic repulsive forces
Ovalbumin
Biomolecules
ovalbumin
article
conformational transition
controlled study
denaturation
electricity
heating
methylation
nonhuman
physical chemistry
priority journal
protein aggregation
protein engineering
surface charge
Animals
Electrostatics
Heat
Kinetics
Ovalbumin
Protein Denaturation
Protein Folding
Urea
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http://resolver.tudelft.nl/uuid:b2f932da-743a-48f3-a90a-189005e7c419
DOI
https://doi.org/10.1021/bm0612283
TNO identifier
239952
ISSN
1525-7797
Source
Biomacromolecules, 8 (5), 1648-1656
Document type
article