Owing to its association with a diverse range of human diseases, the determinants of protein aggregation are studied intensively. It is generally accepted that the effective aggregation tendency of a protein depends on many factors such as folding efficiency towards the native state, thermodynamic stability of that conformation, intrinsic aggregation propensity of the polypeptide sequence and its ability to be recognized by the protein quality control system. The intrinsic aggregation propensity of a polypeptide sequence is related to the presence of short APRs (aggregation-prone regions) that self-associate to form intermolecular β-structured assemblies. These are typically short sequence segments (5–15 amino acids) that display high hydrophobicity, low net charge and a high tendency to form β-structures. As the presence of such APRs is a prerequisite for aggregation, a plethora of methods have been developed to identify APRs in amino acid sequences. In the present chapter, the methodological basis of these approaches is discussed, as well as some practical applications.
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August 2014
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Review Article|
August 18 2014
Predicting aggregation-prone sequences in proteins
Greet De Baets
;
Greet De Baets
*Switch Laboratory, VIB, University of Leuven, Herestraat 49 Box 802, 3000 Leuven, Belgium
†Switch Laboratory, Department of Cellular and Molecular Medicine, University of Leuven, B-3000 Leuven, Belgium
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Joost Schymkowitz
;
Joost Schymkowitz
1
*Switch Laboratory, VIB, University of Leuven, Herestraat 49 Box 802, 3000 Leuven, Belgium
†Switch Laboratory, Department of Cellular and Molecular Medicine, University of Leuven, B-3000 Leuven, Belgium
1Correspondence may be addressed to either of these authors (email joost.schymkowitz@switch.vib-kuleuven.be or frederic.rousseau@switch.vib-kuleuven.be).
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Frederic Rousseau
Frederic Rousseau
1
*Switch Laboratory, VIB, University of Leuven, Herestraat 49 Box 802, 3000 Leuven, Belgium
†Switch Laboratory, Department of Cellular and Molecular Medicine, University of Leuven, B-3000 Leuven, Belgium
1Correspondence may be addressed to either of these authors (email joost.schymkowitz@switch.vib-kuleuven.be or frederic.rousseau@switch.vib-kuleuven.be).
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Essays Biochem (2014) 56: 41–52.
Citation
Sarah Perrett, Greet De Baets, Joost Schymkowitz, Frederic Rousseau; Predicting aggregation-prone sequences in proteins. Essays Biochem 18 August 2014; 56 41–52. doi: https://doi.org/10.1042/bse0560041
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