The folding of proteins that contain disulfide bonds is termed oxidative protein folding. It involves a chemical reaction resulting in the formation of disulfide bonds and a physical conformational folding reaction that promotes the formation of the native structure. While the presence of disulfide bonds significantly increases the complexity of the folding landscape, it is generally recognized that native disulfide bonds help funnel the trajectory towards the final folded form. Here, we review the role of disulfide bonds in oxidative protein folding and argue that even structure-inducing native disulfide bond formation treads a fine line in the regeneration of disulfide-bond-containing proteins. The translation of this observation to protein misfolding related disorders is discussed.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/s10930-021-09976-7 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
A motion-responsive injectable lubricative hydrogel for efficient Achilles tendon adhesion prevention.
Mater Today Bio
February 2025
Basic Research Key Laboratory of General Surgery for Digital Medicine, Affiliated Hospital of Hebei University, Baoding, 071000, China.
Achilles tendon is a motor organ that is prone to tissue adhesion during its repair process after rupture. Therefore, developing motion-responsive and anti-adhesive biomaterials is an important need for the repair of Achilles tendon rupture. Here, we report an injectable lubricative hydrogel (ILH) based on hydration lubrication mechanism, which is also motion-responsive based on sol-gel reversible transmission.
View Article and Find Full Text PDFIdentification of disulfide bond-linking sites in biosynthesized platelet factor 4 by establishing a partial reduction method without alkylation.
Anal Methods
January 2025
College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, P.R. China.
Platelet factor 4 (PF4), a specific protein primarily found in megakaryocytes and platelet α-granules, plays an essential role in the coagulation process. It carries a high positive charge and thus has a unique ability to readily form complexes with negatively charged heparin. This interaction between PF4 and heparin plays a crucial role in platelet aggregation and thrombosis, resulting in heparin-induced thrombocytopenia (HIT).
View Article and Find Full Text PDFPre-folding purification procedures for inclusion body-derived non-tagged cationic recombinant proteins with multiple disulfide bonds for efficient refolding.
Biotechnol Prog
January 2025
Graduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
The production of disulfide-containing recombinant proteins often requires refolding of inclusion bodies before purification. A pre-refolding purification step is crucial for effective refolding because impurities in the inclusion bodies interfere with refolding and subsequent purification. This study presents a new pre-refolding procedure using a reversible S-cationization technique for protein solubilization and purification by reversed-phase high performance liquid chromatography.
View Article and Find Full Text PDFLight chain Split Luciferase assay implicates pathological NOTCH3 thiol reactivity in inherited cerebral small vessel disease.
J Biol Chem
January 2025
Departments of Neurology, University of Michigan, Ann Arbor, MI 48109; Departments of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI 48109; Neurology Service, VA Ann Arbor Healthcare System, Department of Veterans Affairs, Ann Arbor, MI 48105. Electronic address:
Stereotyped mutations in NOTCH3 drive CADASIL, the leading inherited cause of stroke and vascular dementia. The vast majority of these mutations result in alterations in the number of cysteines in the gene product. However, non-cysteine altering pathogenic mutations have also been identified, making it challenging to discriminate pathogenic from benign NOTCH3 sequence variants.
View Article and Find Full Text PDFBacterial expression, purification and characterization of the human Dectin-1 lectin domain for structural and functional studies.
Protein Expr Purif
January 2025
Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi 981-8558, Japan. Electronic address:
Dectin-1 (CLEC7A), a C-type lectin-like receptor that recognizes β-1,3 glucans, has a key role in the innate immune system. While the lectin domain of mouse Dectin-1 has been solubilized and refolded from inclusion bodies in Escherichia coli, similar refolding of the human Dectin-1 lectin domain is hindered by the formation of misfolded multimers with aberrant intermolecular disulfide bonds. The aim of this study was to develop a method for the large-scale production of the human Dectin-1 lectin domain.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!