Key result
The R502W mutant of cardiac myosin binding protein C exhibited lower stability of its hydrophobic core compared to the wild-type form, potentially reducing its ability to return to its initial structure after external stretching.
The R502W mutation in cardiac myosin binding protein C reduces the stability of its hydrophobic core, potentially impairing its ability to recover from mechanical stretching.
Cardiac myosin binding protein C is the object of analysis presented in this paper. The fuzzy oil drop model was applied to analyze the status of the hydrophobic core in two forms of this protein: WT and R502W mutant. The status of the mutant is revealed to be of lower stability than the WT form. The high order of the hydrophobic core is interpreted as the factor of stability of the tertiary structure. The muscle proteins, which undergo significant structural changes as the consequence of external stretching forces, are expected to return to initial structures after the release of an external force. The mutant R502W appears to represent lower stability; thus, the return to the initial structure may be of lower probability. The comparable analysis to other muscle domains (titin) and immunoglobulin domains suggests the very subtle relation to the biological activity of these proteins.
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Golda et al. (2017) studied this question. R502W mutation vs. Wild-type (WT) form was evaluated on Status of the hydrophobic core and stability of the tertiary structure. The R502W mutant of cardiac myosin binding protein C exhibited lower stability of its hydrophobic core compared to the wild-type form, potentially reducing its ability to return to its initial structure after external stretching.
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