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Association between foldability and aggregation propensity in small disulfide-rich proteins
Hugo Fraga1, Ricardo Graña-Montes, Ricard Illa
1Departament de Bioquimica i Biologia Molecular, Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona , Barcelona, Spain .
Antioxidants & Redox Signaling
|March 19, 2014
Summary
Disulfide-rich domains (DRDs) exhibit intrinsic disorder, similar to intrinsically disordered proteins (IDPs). This disorder influences their folding pathways and prevents aggregation before disulfide bonds form.
Area of Science:
- Protein Biochemistry
- Structural Biology
- Biophysics
Background:
- Disulfide-rich domains (DRDs) are small proteins stabilized by disulfide bonds.
- Many DRDs unfold upon reduction, suggesting inherent disorder.
- DRDs perform diverse biological functions.
Purpose of the Study:
- To analyze the degree of intrinsic disorder in 97 representative DRDs.
- To investigate the relationship between protein disorder, folding, and aggregation propensities in DRDs.
Main Methods:
- Sequence analysis to predict disordered regions.
- Assessment of aggregation propensity.
- Comparison with intrinsically disordered proteins (IDPs) and globular domains.
Main Results:
- Many DRDs are predicted to be intrinsically disordered proteins (IDPs) or contain disordered regions.
- DRDs exhibit lower aggregation propensity and higher solubility compared to other globular domains.
- This suggests an evolutionary adaptation to avoid aggregation before achieving their native structure.
Conclusions:
- DRDs resemble IDPs in their reduced state and become globular upon disulfide bond formation.
- Protein folding and aggregation propensities are intrinsically linked.
- These properties dictate the folding pathways of DRDs to their native oxidized states.
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