Transition of intrinsically unfolded α-synuclein into the fibrillar state 
characterized by NMR spectroscopy.

Cho, M. K.

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Transition of intrinsically unfolded α-synuclein into the fibrillar state characterized by NMR spectroscopy.

Cho, M. K. (2008). Transition of intrinsically unfolded α-synuclein into the fibrillar state characterized by NMR spectroscopy. PhD Thesis, Universität Göttingen, Göttingen.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-DA91-E Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0027-EEFE-B

Genre: Thesis

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http://ediss.uni-goettingen.de/bitstream/handle/11858/00-1735-0000-0006-ACB9-3/cho.pdf?sequence=1 (Publisher version) Open Access status unknown

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Creators:
Cho, M. K.¹, Author

Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571

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Language(s): eng - English

Dates: Accepted: 2008-10-28

Publication Status: Accepted / In Press

Pages: -

Publishing info: Göttingen : Universität Göttingen

Table of Contents: -

Rev. Type: -

Identifiers: eDoc: 419112
URI: http://webdoc.sub.gwdg.de/diss/2008/cho/cho.pdf

Degree: PhD

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