Min-Kyu Cho (2004 - 2007)

++49 - 551 - 201 2219 e-mail Max-Planck-Institut für Biophysikalische Chemie NMR based Structural Biology Am Faßberg 11 37077 Göttingen Germany

• Transition mechanism of soluble healthy α-synuclein into the fibrillar state leading to Parkinson's disease
• Spectroscopic methods characterizing biomolecular interactions
• Methodology in NMR sepctroscopy

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α-synuclein (αS) undergoes dramatic conformation change from unfolded monomer to well structured amyloid fibril. Electron microscopy (EM) pictures show clusters of monomers and amyloid fibril from the same αS. By nuclear magnetic resonance (NMR) spectroscopy, dynamic change of each amino acid in monomer can be investigated. The graph showed the differences of residual dipolar couplings (RDC) between αS in physiological condition and that in aggregation enhanced condition (low pH).

PCGG activities

Cooperation(s):

• Bögehold - Abel group (BM8)
• Hachenberg - Samwer group (BM8)

• Analytical laser induced liquid beam desorption mass spectrometry of biomolecules and their aggregates (January 2006)
  

• Project Week in the Abel Group: Analytical laser induced liquid beam desorption mass spectrometry of biomolecules and their aggregates

• ♦ M. K. Cho, H. Y. Kim, P. Bernado, C. O. Fernandez, M. Blackledge, M. Zweckstetter, Amino Acid Bulkiness Defines the Local Conformations and Dynamics of Natively Unfolded alpha-Synuclein and Tau., J. Am. Chem. Soc. 2007, 129(11), 3032.
• ♦ L. Skora, M. K. Cho, H. Y. Kim, S. Becker, C. O. Fernandez, M. Blackledge, M. Zweckstetter, Charge-Induced Molecular Alignment of Intrinsically Disordered Proteins, Angew. Chem. Int. Ed. 2006, 45(42), 7012-7015.
• ♦ R. Jauch, M. K. Cho, S. Jakel, C. Netter, K. Schreiter, B. Aicher, M. Zweckstetter, H. Jackle, M. C. Wahl, Mitogen-activated protein kinases interacting kinases are autoinhibited by a reprogrammed activation segment, Embo J. 2006, 25(17), 4020-4032.

• Poster: May 24 2007 Amino Acid Bulkiness Defines the Local Conformations and Dynamics of Natively Unfolded α-Synuclein and Tau (EMBO IUP meeting)
• Poster: April 26 2007 Amino Acid Bulkiness Defines the Local Conformations and Dynamics of Natively Unfolded α-Synuclein (48th ENC)
• Talk: Mar 19 2007 Structural characterization of alpha-synuclein aggregation by NMR spectroscopy (9th Workshop)
• Poster: Oct 09 2006 Conformation of a partially folded intermediate in alpha-synuclein fibrillation (Eighth Workshop 2006)
• Poster: Aug 22 2006 Conformation of a partially folded intermediate in alpha-synuclein fibrillation (XXIIth ICMRBS)
• Poster: Mar 21 2006 High-resolution characterization of α-synuclein misfolding (Review Colloquium)
• Poster: Mar 08 2006 Structural characterization of α-synuclein conformation change (Seventh Workshop 2006
  Spectroscopy and Dynamics of Molecular Coils and Aggregates (Göttingen - Paris))
• Poster: Sept 05 2005 NMR investigation on conformation change of α-synuclein from monomer to aggregate (Sixth Workshop 2005)
• Organization: April 06 2005 Host student of H.-H. Limbach (Fifth Workshop = 91st Bunsen Colloquium 2005)
• Poster: April 06 2005 Structural characterization of a-Synuclein conformation change in atomic resolution by NMR spectroscopy (Fifth Workshop = 91st Bunsen Colloquium 2005)
• Talk: Nov 03 2004 NMR Study on TA0743 and Exploring Protein Fold Space Using Data Distribution Method on Grid Platform (Seminar WS 2004/2005)