ArticleProteins2017
Temperature stability of proteins: Analysis of irreversible denaturation using isothermal calorimetry.
Article in Proteins, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Initiating radical polymerization at room temperature: Why and How?RSC advances · 2026Review
- Search for effective bacteriolytic enzymes and their combinations for the treatment of polymicrobial biofilm-associated infections.World journal of microbiology & biotechnology · 2026Article
- Conformational landscapes of rigid and flexible molecules explored with variable temperature ion mobility-mass spectrometry.Nature communications · 2025Article
- Temperature induces brain-intake shift of recombinant high-density lipoprotein after traumatic brain injury.Journal of nanobiotechnology · 2024Article
- Temperature-Dependent Cytokine Neutralization Induced by Magnetoelectric Nanoparticles: An In Silico Study.International journal of molecular sciences · 2024Article
- Extrapolating differential scanning calorimetry data for monoclonal antibodies to low temperatures.Analytical biochemistry · 2024Article
- Addition of sodium malonate alters the morphology and increases the critical flux during tangential flow filtration of precipitated immunoglobulins.Protein science : a publication of the Protein Society · 2024Article
- One-pot DTECT enables rapid and efficient capture of genetic signatures for precision genome editing and clinical diagnostics.Cell reports methods · 2024Article
- Stabilization challenges and aggregation in protein-based therapeutics in the pharmaceutical industry.RSC advances · 2023Review
- Article
- Comparative Studies of Different Preservation Methods and Relative Freeze-Drying Formulations for Extracellular Vesicle Pharmaceutical Applications.ACS biomaterials science & engineering · 2023Article
- Development of a Bioreactor-Coupled Flow-Cell Setup for 3D In Situ Nanotomography of Mg Alloy Biodegradation.ACS applied materials & interfaces · 2023Article
- The Effect of Argon Plasma Surface Treatment on Poly(lactic-co-glycolic acid)/Collagen-Based Biomaterials for Bone Tissue Engineering.Biomimetics (Basel, Switzerland) · 2022Article
- A Biopharmaceutical Perspective on Higher-Order Structure and Thermal Stability of mRNA Vaccines.Molecular pharmaceutics · 2022Review
- Integrated Multifunctional Graphene Discs 2D Plasmonic Optical Tweezers for Manipulating Nanoparticles.Nanomaterials (Basel, Switzerland) · 2022Article
- Fever temperatures impair hemolysis caused by strains ofHeliyon · 2022Article
- Amyloid Self-Assembly of Lysozyme in Self-Crowded Conditions: The Formation of a Protein Oligomer Hydrogel.Biomacromolecules · 2021Article
- Article
- Single-walled carbon nanotubes as a photo-thermo-acoustic cancer theranostic agent: theory and proof of the concept experiment.Scientific reports · 2020Article
- Following Structural Changes by Thermal Denaturation Using Trapped Ion Mobility Spectrometry-Mass Spectrometry.The journal of physical chemistry. B · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The structural stability of proteins has been traditionally studied under conditions in which the folding/unfolding reaction is reversible, since thermodynamic parameters can only be determined under these conditions. Achieving reversibility conditions in temperature stability experiments has often required performing the experiments at acidic pH or other nonphysiological solvent conditions. With the rapid development of protein drugs, the fastest growing segment in the pharmaceutical industry, the need to evaluate protein stability under formulation conditions has acquired renewed urgency. Under formulation conditions and the required high protein concentration (∼100 mg/mL), protein denaturation is irreversible and frequently coupled to aggregation and precipitation. In this article, we examine the thermal denaturation of hen egg white lysozyme (HEWL) under irreversible conditions and concentrations up to 100 mg/mL using several techniques, especially isothermal calorimetry which has been used to measure the enthalpy and kinetics of the unfolding and aggregation/precipitation at 12°C below the transition temperature measured by DSC. At those temperatures the rate of irreversible protein denaturation and aggregation of HEWL is measured to be on the order of 1 day
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