Skip to main content

Structure Solution of Misfolded Conformations Adopted by Intrinsically Disordered Alzheimer's Tau Protein

Buy Article:

$55.00 plus tax (Refund Policy)

Until now it was impossible to obtain atomic structure of intrinsically disordered protein (IDP) tau and/or its assembly in Alzheimer's paired helical filaments as neither of them could have been prepared in the form amenable to Xray or NMR techniques. Using IDP tau property to attain regular tertiary structure after binding events during selfassembly or when complexed with its target we propose monoclonal antibodies as surrogate tau protein binding partners to form complexes and crystals for structure solution by X-ray technique.

No References
No Citations
No Supplementary Data
No Data/Media
No Metrics

Keywords: Alzheimer's disease; crystal structure; intrinsically disordered protein; monoclonal antibody; tau protein

Document Type: Research Article

Publication date: 2009-01-01

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more