Veronika Džupponová

ORCID: 0000-0003-3127-5376
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About
Contact & Profiles
Research Areas
  • Monoclonal and Polyclonal Antibodies Research
  • Protein purification and stability
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Glycosylation and Glycoproteins Research
  • Advanced Electron Microscopy Techniques and Applications
  • Polymer Surface Interaction Studies
  • RNA and protein synthesis mechanisms
  • Drug Transport and Resistance Mechanisms
  • Protein Interaction Studies and Fluorescence Analysis
  • RNA modifications and cancer

University of Pavol Jozef Šafárik
2020-2024

Bioscience (Slovakia)
2024

Institute of Physics of the Slovak Academy of Sciences
2022

X-ray crystallography is an established tool to probe the structure of macromolecules with atomic resolution. Compared alternative techniques such as single-particle cryo-electron microscopy and micro-electron diffraction, uniquely suited room-temperature studies for obtaining a detailed picture subjected external electric field (EEF). The impact EEF on proteins has been extensively explored through single-crystal crystallography, which works well larger high-quality protein crystals. This...

10.1107/s1600576724002140 article EN cc-by Journal of Applied Crystallography 2024-04-15

Thermophilic proteins and enzymes are attractive for use in industrial applications due to their resistance against heat denaturants. Here, we report on a thermophilic protein that is stable at high temperatures (Ttrs, hot 67 °C) but undergoes significant unfolding room temperature cold denaturation. Little known about the denaturation of proteins, although it can significantly limit applications. We investigated multidomain translation initiation factor 2 (IF2) from Thermus thermophilus....

10.3390/ijms24076787 article EN International Journal of Molecular Sciences 2023-04-05

Protein aggregation is one of the most critical processes affecting protein solubility in various contexts-from therapeutics formulation to diseases. In general, time-dependent changes are complex kinetically driven that often involve a triggering event consists unfolding/misfolding followed by assembling aggregation-competent species. this study, we have examined relation between stability and recombinant human antibody light chain, hLC, which was found form renal tubular casts multiple...

10.1002/pro.3968 article EN Protein Science 2020-10-08
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