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(b) safety and stability

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DSC-based analysis of the C-terminal domain of chicken gizzard caldesmon CaD, (CaD 136 , residues 636771) and series of its single tryptophan mutants (W674A, W707A, and W737A) and a double tryptophan mutant (W674A/W707A) revealed that all these proteins are characterized by high specific heat capacity values (ranging from 23 J/(g K)) and the absence of distinct heat absorption peaks within the temperature region from 10 to 100 C suggested that their structure is predominantly unfolded (Permyakov et al., 2015)

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