Title
Role of the hydrophobic core in cytoskeleton protein: cardiac myosin binding protein C.
Abstract
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.
Year
DOI
Venue
2017
10.1515/bams-2017-0018
BIO-ALGORITHMS AND MED-SYSTEMS
Keywords
Field
DocType
cardiac myosin,hydrophobicity,hypertrophic cardiomyopathy,immunoglobulin,muscle proteins,titin
Myosin-binding protein C,Cytoskeleton,Titin,Cell biology,Chemistry,Myosin light-chain kinase,Rho-associated protein kinase,Hypertrophic cardiomyopathy,Antibody
Journal
Volume
Issue
ISSN
13
3
1895-9091
Citations 
PageRank 
References 
0
0.34
1
Authors
6
Name
Order
Citations
PageRank
Maria Golda100.34
Mateusz Banach278.88
Zdzislaw Wisniowski300.34
Wojciech Ziajka400.34
Leszek Konieczny56722.55
Irena Roterman67830.08