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

Myeongsang Lee, Inchul Baek, Hyunsung Choi, Jae In Kim, Sungsoo Na

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


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
Issue number3
Publication statusPublished - 2015 Oct 23

Bibliographical note

Funding Information:
S.N. gratefully acknowledges the Basic Science Research Program, through the National Research Foundation of Korea (NRF) and funded by the Ministry of Science, ICT & Future Planning (MSIP) (No. 2007–0056094 and No. 2014R1A2A1A11052389 ).

Publisher Copyright:
© 2015 Elsevier Inc. All rights reserved.


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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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