Abstract
The effects of amino acid substitutions E90K, N98S and A149V in the light chain of neurofilaments (NFL) on the structure and thermal denaturation of the NFL molecule was investigated. By using the circular dichroism spectroscopy, it was shown that these substitutions do not lead to a changes in the α-helical structure of NFL, but they caused a noticeable effects on the stability of the molecule. We also identified calorimetric domains in the NFL structure by using the differential scanning calorimetry. It was shown that the E90K replacement lead to the disappearance of the low-temperature thermal transition (domain 1). The mutations lead to changes in the enthalpy of melting of NFL domains, as well as lead to significant changes in the melting temperatures (Tm) of some calorimetric domains. Thus, despite the fact that all these amino acid substitutions are associated with the development of Charcot-Marie-Tooth neuropathy, and two of them are even located very close to each other in the coiled-coil domain 1A, they differently effects on the structure and stability of the NFL molecule.
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