ArticleScientific reports2018
The extreme hyper-reactivity of Cys94 in lysozyme avoids its amorphous aggregation.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
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- The unusual properties of lactoferrin during its nascent phase.Scientific reports · 2023Article
- The Anfinsen Dogma: Intriguing Details Sixty-Five Years Later.International journal of molecular sciences · 2022Article
- Injectable Hydrogel Based on Protein-Polyester Microporous Network as an Implantable Niche for Active Cell Recruitment.Pharmaceutics · 2022Article
- Oxidative Folding of Proteins: The "Smoking Gun" of Glutathione.International journal of molecular sciences · 2021Review
- Effect of PCSK9 inhibitors on pulse wave velocity and monocyte-to-HDL-cholesterol ratio in familial hypercholesterolemia subjects: results from a single-lipid-unit real-life setting.Acta diabetologica · 2021Observational
- New Factors Enhancing the Reactivity of Cysteines in Molten Globule-Like Structures.International journal of molecular sciences · 2020Article
- Ultra-rapid glutathionylation of chymotrypsinogen in its molten globule-like conformation: A comparison to archaeal proteins.Scientific reports · 2020Article
- Ultra-Rapid Glutathionylation of Ribonuclease: Is this the Real Incipit of its Oxidative Folding?International journal of molecular sciences · 2019Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many proteins provided with disulfide bridges in the native state undergo amorphous irreversible aggregation when these bonds are not formed. Here we show that egg lysozyme displays a clever strategy to prevent this deleterious aggregation during the nascent phase when disulfides are still absent. In fact, when the reduced protein assembles into a molten globule state, its cysteines acquire strong hyper-reactivity towards natural disulfides. The most reactive residue, Cys94, reacts with oxidized glutathione (GSSG) 3000 times faster than an unperturbed protein cysteine. A low pK
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