| Autor: |
Nefedova VV; Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia., Kleymenov SY; Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia.; Koltzov Institute of Developmental Biology, Russian Academy of Sciences, 119334 Moscow, Russia., Safenkova IV; Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia., Levitsky DI; Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia., Matyushenko AM; Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia. |
| Jazyk: |
angličtina |
| Zdroj: |
Biomolecules [Biomolecules] 2024 Jan 09; Vol. 14 (1). Date of Electronic Publication: 2024 Jan 09. |
| DOI: |
10.3390/biom14010085 |
| Abstrakt: |
Neurofilaments are neuron-specific proteins that belong to the intermediate filament (IFs) protein family, with the neurofilament light chain protein (NFL) being the most abundant. The IFs structure typically includes a central coiled-coil rod domain comprised of coils 1A, 1B, and 2, separated by linker regions. The thermal stability of the IF molecule plays a crucial role in its ability for self-association. In the current study, we investigated the thermal stability of NFL coiled-coil domains by analyzing a set of recombinant domains and their fusions (NFL 1B , NFL 1A+1B , NFL 2 , NFL 1B+2 , and NFL ROD ) via circular dichroism spectroscopy and differential scanning calorimetry. The thermal stability of coiled-coil domains is evident in a wide range of temperatures, and thermal transition values (T m ) correspond well between isolated coiled-coil domains and full-length NFL. NFL 1B has a T m of 39.4 °C, and its' fusions, NFL 1A+1B and NFL 1B+2 , have a T m of 41.9 °C and 41.5 °C, respectively. However, in the case of NFL 2 , thermal denaturation includes at least two thermal transitions at 37.2 °C and 62.7 °C. These data indicate that the continuous α-helical structure of the coil 2 domain has parts with varied thermal stability. Among all the NFL fragments, only NFL 2 underwent irreversible heat-induced denaturation. Together, these results unveil the origin of full-length NFL's thermal transitions, and reveal its domains structure and properties. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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