ArticleBiophysical journal2006
How aggregation and conformational scrambling of unfolded states govern fluorescence emission spectra.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
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- Revisiting fatty acid-mediated antibody purification from plasma with insights into selectivity and protein integrity.PloS one · 2026Article
- Biophysical insights into recombinant Zeocin binding protein: conformational stability and folding dynamics across pH and temperature.Frontiers in molecular biosciences · 2026Article
- Thermal denaturation of porcine myofibrillar proteins at different heating temperatures: A focus on the surface hydrophobicity.Food chemistry: X · 2025Article
- A conserved H-bond network in human aquaporin-1 is necessary for native folding and oligomerization.Biophysical journal · 2024Article
- Doxorubicin as a Drug Repurposing for Disruption of α-Chymotrypsinogen-A Aggregates.The protein journal · 2024Article
- Online monitoring of protein refolding in inclusion body processing using intrinsic fluorescence.Analytical and bioanalytical chemistry · 2024Article
- Thr-to-Ala Mutation Leads to a Larger Aromatic Pair and Reduced Packing Density in α1,α3-Helices during Thioredoxin Cold Adaptation.ACS omega · 2024Article
- Impact of Urea on Monoclonal Antibodies: Multiple Destabilization and Aggregation Effects for Therapeutic Immunoglobulin G Proteins.ACS omega · 2024Article
- Fluorescence-Based Protein Stability Monitoring-A Review.International journal of molecular sciences · 2024Review
- Isothermal chemical denaturation assay for monitoring protein stability and inhibitor interactions.Scientific reports · 2023Article
- Thermostable protein-stabilized gold nanoclusters as a peroxidase mimic.Nanoscale advances · 2023Article
- The unusual properties of lactoferrin during its nascent phase.Scientific reports · 2023Article
- Multiplexed RNA profiling by regenerative catalysis enables blood-based subtyping of brain tumors.Nature communications · 2023Article
- The effect of novel antihypertensive drug valsartan on lysozyme aggregation: A combined in situ and in silico study.Heliyon · 2023Article
- State-of-the-art and novel approaches to mild solubilization of inclusion bodies.Frontiers in bioengineering and biotechnology · 2023Review
- Investigation of Aggregation and Disaggregation of Self-Assembling Nano-Sized Clusters Consisting of Individual Iron Oxide Nanoparticles upon Interaction with HEWL Protein Molecules.Nanomaterials (Basel, Switzerland) · 2022Article
- Thermal Shift Assay for Small GTPase Stability Screening: Evaluation and Suitability.International journal of molecular sciences · 2022Article
- Influence of Urea and Dimethyl Sulfoxide on K-Peptide Fibrillation.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In a case study on five homologous alpha-amylases we analyzed the properties of unfolded states as obtained from treatments with GndHCl and with elevated temperatures. In particular the wavelength of the tryptophan fluorescence emission peak (lambda(max)) is a valuable parameter to characterize properties of the unfolded state. In all cases with a typical red shift of the emission spectrum occurring during structural unfolding we observed a larger magnitude of this shift for GndHCl-induced unfolding as compared to thermal unfolding. Although a quantitative relation between aggregation and reduction of the unfolding induced red shifts cannot be given, our data indicate that protein aggregation contributes significantly to smaller magnitudes of red shifts as observed during thermal unfolding. In addition, other properties of the unfolded states, most probable structural compactness or simply differences in the conformational scrambling, also affect the magnitude of red shifts. For the irreversible unfolding alpha-amylases studied here, transition temperatures and magnitudes of red shifts are strongly depending on heating rates. Lower protein concentrations and smaller heating rates lead to larger red shifts upon thermal unfolding, indicating that under these conditions the protein aggregation is less pronounced.
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