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Article

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 & dynamics - 1 Sept 2017

Ali Shabana Kouser, Sneha P, Priyadharshini Christy J, Zayed Hatem, George Priya Doss C

Abstract excerpt

Mutations 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...

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Source

Identifiers

PMID: 27677677
DOI: 10.1080/07391102.2016.1229634

Genes

FGG

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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