Role of the hydrophobic core in cytoskeleton protein: cardiac myosin binding protein C

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. Th...

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Published inBio-algorithms and med-systems Vol. 13; no. 3; pp. 161 - 165
Main Authors Gołda, Maria, Banach, Mateusz, Wiśniowski, Zdzisław, Ziajka, Wojciech, Konieczny, Leszek, Roterman, Irena
Format Journal Article
LanguageEnglish
Published Berlin De Gruyter 26.09.2017
Walter de Gruyter GmbH
Subjects
Biological activity
cardiac myosin
Domains
Hydrophobicity
hypertrophic cardiomyopathy
immunoglobulin
muscle proteins
Muscles
Myosin
Proteins
Structural stability
titin
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Summary: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.
ISSN:1895-9091
1896-530X
DOI:10.1515/bams-2017-0018