A molecular journey to check the conformational dynamics of tau tubulin kinase 2 mutations associated with Alzheimer's disease.

ABSTRACT: Proteins are one of the most vital components of biological functions. Proteins have evolutionarily conserved structures as the shape and folding pattern predominantly determine their function. Considerable research efforts have been made to study the protein folding mechanism. The misfolding of protein intermediates of large groups form polymers with unwanted aggregates that may initiate various diseases. Amongst the diseases caused by misfolding of proteins, Alzheimer's disease (AD) is one of the most prevalent neuro-disorders which has a worldwide impact on human health. The disease is associated with several vital proteins and single amino acid mutations. Tau tubulin kinase 2 (TTBK2) is one of the kinases which is known to phosphorylate tau and tubulin. The literature strongly supports

SUBMITTER: Ahamad S 

PROVIDER: S-EPMC8693565 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature