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AuthorAli, Shabana Kouser
AuthorSneha, P
AuthorPriyadharshini Christy, J
AuthorZayed, Hatem
AuthorGeorge Priya Doss, C
Available date2017-10-11T06:58:23Z
Publication Date2016-09-27
Publication Namejournal of biomolecular structure and dynamicsen_US
Identifierhttp://dx.doi.org/10.1080/07391102.2016.1229634
CitationShabana Kouser Ali, P. Sneha, J. Priyadharshini Christy, Hatem Zayed & C. George Priya Doss (2017) Molecular dynamics-based analyses of the structural instability and secondary structure of the fibrinogen gamma chain protein with the D356V mutation, Journal of Biomolecular Structure and Dynamics, 35:12, 2714-2724, DOI: 10.1080/07391102.2016.1229634
ISSN0739-1102
URIhttp://hdl.handle.net/10576/5681
AbstractMutations in the fibrinogen gamma chain (FGG) gene have been associated with various disorders, such as dysfibrinogenemia, thrombophilia, and hypofibrinogenemia. A literature survey showed that a residue exchange in fibrinogen Milano I from γ Asp to Val at position 330 impairs fibrin polymerization. The D356V (D330V) mutation located in the C-terminus was predicted to be highly deleterious and to affect the function of the protein. The pathogenicity of the altered gene and changes in protein functions were predicted using in silico methods, such as SIFT, PolyPhen 2, I-Mutant 3.0, Align GV-GD, PhD-SNP, and SNPs&GO. The secondary structure of the mutant protein was unwound by the end of the 50-ns simulation period, and a structural change in the helix-turn transition of the alpha-helical (352-356) region residues was observed. Moreover, a change in the length of the helical region was visualized in the mutant trajectory file, indicating the local transient unfolding of the protein. The obtained computational results suggest that the substitution of the neutral amino acid valine for the acidic amino acid aspartic acid at position 356 results in an unwound conformation within 50 ns, which might contribute to defective polymerization. Our analysis also provides insights into the effect of the conformational change in the D356V (D330V) mutant on protein structure and function.
Languageen
PublisherTaylor & Francis
SubjectD356V (D330V)
SubjectFGG
Subjectmolecular simulation
Subjectsecondary structure
Subjectsingle nucleotide polymorphism
TitleMolecular dynamics-based analyses of the structural instability and secondary structure of the fibrinogen gamma chain protein with the D356V mutation.
TypeArticle
Pagination2714–2724
Issue Number12
Volume Number35
dc.identifier.essn 1538-0254


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