Effects of lysine residues on structural characteristics and stability of tau proteins

Myeongsang Lee, Inchul Baek, Hyunsung Choi, Jae In Kim, Sung Soo Na

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Pathological amyloid proteins have been implicated in neuro-degenerative diseases, specifically Alzheimer's, Parkinson's, Lewy-body diseases and prion related diseases. In prion related diseases, functional tau proteins can be transformed into pathological agents by environmental factors, including oxidative stress, inflammation, Aβ-mediated toxicity and covalent modification. These pathological agents are stable under physiological conditions and are not easily degraded. This un-degradable characteristic of tau proteins enables their utilization as functional materials to capturing the carbon dioxides. For the proper utilization of amyloid proteins as functional materials efficiently, a basic study regarding their structural characteristic is necessary. Here, we investigated the basic tau protein structure of wild-type (WT) and tau proteins with lysine residues mutation at glutamic residue (Q2K) on tau protein at atomistic scale. We also reported the size effect of both the WT and Q2K structures, which allowed us to identify the stability of those amyloid structures.

Original languageEnglish
Pages (from-to)486-492
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume466
Issue number3
DOIs
Publication statusPublished - 2015 Aug 8

Keywords

  • Amyloid proteins
  • Lysine mutation
  • Molecular dynamics
  • Size effects
  • Tau protein

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

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