Meanings of thermal denaturation in English

The mutant alphaB-crystallin was more susceptible than wild-type to thermal denaturation.

The modifications were probed by UV & Fluorescence spectroscopy, thermal denaturation and hydroxyapatite chromatography.

Among the hits, an in vitro assay identified one molecule that stabilized retromer against thermal denaturation.

Modified duplexes showed dramatically enhanced stability to serum nucleases, and were characterized by circular dichroism and thermal denaturation studies.

The midpoint of thermal denaturation of L94F mutant is 17°C less than wild type.

This modification has been shown to confer resistance to thermal denaturation for CBH-1 and EG-1 cellulases.

In previous research papers, DSC profiles from blood samples of patients were analyzed and they exhibited marked differences in the thermal denaturation profile.

Furthermore, thermal denaturation studies revealed a decrease of 4.3°C in the Tm value of ΔmALAS2, implicating lower thermal stability.

Thermal denaturation studies in benign media indicated that the lactam-based peptides were very stable.

Thermal denaturation has irreversible destabilizing effects on both proteins, yet reveals important functional details regarding substrate accessibility to the buried active site.

Thermal denaturation experiments of coiled-coil forming NMIIA fragments indicate that the coiled-coil partially unwinds upon S100A4 binding.

Thermal denaturation studies show that a specific two amino acid (Gly-Leu) extension at the C-terminus is primarily responsible for a significant increase in stability.