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oai:www.ideals.illinois.edu:2142/29544 2023-07-10 col_2142_14789 col_2142_5131 com_2142_14788 com_2142_8903 com_2142_5130

http://hdl.handle.net/2142/29544 en Rienstra, Chad M. Oldfield, Eric Schulten, Klaus J. George, Julia M. Nieuwkoop, Andrew 2012-02-01T00:54:45Z 2014-02-01T11:00:23Z 2011-12 2012-02-01T00:54:45Z 2011-12 Solid state NMR (SSNMR) is a structure determination technique uniquely suited to study protein aggregates and fibrils. Unlike solution NMR or X-ray crystallography, SSNMR can obtain atomic resolution structural information on samples of protein fibrils which are insoluble and do not produce X-ray diffracting crystals. As SSNMR begins to realize this potential, new structure determination techniques will be important in enable SSNMR to investigate ever larger and more complicated systems. Alpha-synuclein (AS) is the primary protein component of Lewy bodies, the pathological hallmark of Parkinson’s disease. The structure of AS in its fibril form is unknown, as is the mechanism by which it contributes to neurodegeneration. At 140 residues, AS is much larger than other fibril systems that have been studied by SSNMR. To solve the structure of AS fibrils will require combining new pulse sequences with advanced isotopic labeling schemes, and novel structure calculation methods. The techniques developed in this study will be useful in the study of other protein aggregates, as well as membrane proteins and complexes, for which SSNMR is the structure determination method of choice. Item withdrawn by Mark Zulauf (zulauf@illinois.edu) on 2011-11-18T18:56:46Z Item was in collections: University of Illinois Theses & Dissertations (ID: 1) No. of bitstreams: 2 Nieuwkoop_Thesis_finalv3.doc: 10161152 bytes, checksum: 4b1455aab13fbe1df8e88ac7c497606f (MD5) Nieuwkoop_Andrew.pdf: 22351238 bytes, checksum: f3fc38a81acff924b7fa5f678b4ec30f (MD5) Made available in DSpace on 2012-02-01T00:54:45Z (GMT). No. of bitstreams: 3 Nieuwkoop_Andrew.pdf: 22677564 bytes, checksum: f51f0d0bd5a3badf8e6e49e7b646c6ae (MD5) license.txt: 4066 bytes, checksum: baa793ffbebf1c85d069d840f7aaea0d (MD5) Nieuwkoop_Thesis_finalv4.doc: 10163712 bytes, checksum: c942b91ff6c3b39de72a7c00fc1e4cc1 (MD5) Item marked as restricted to the 'Administrator' Group (id=1) by William Ingram (wingram2@illinois.edu) on 2012-02-01T00:57:07Z Item is restricted until 2014-02-01T00:56:58Z Item reinstated by Sarah Shreeves (sshreeve@illinois.edu) on 2014-02-01T11:00:23Z Item was in collections: Dissertations and Theses - Chemistry (ID: 676) Graduate Theses and Dissertations at Illinois (ID: 204) No. of bitstreams: 3 Nieuwkoop_Andrew.pdf: 22677564 bytes, checksum: f51f0d0bd5a3badf8e6e49e7b646c6ae (MD5) license.txt: 4066 bytes, checksum: baa793ffbebf1c85d069d840f7aaea0d (MD5) Nieuwkoop_Thesis_finalv4.doc: 10163712 bytes, checksum: c942b91ff6c3b39de72a7c00fc1e4cc1 (MD5) Item released from any restrictions by Sarah Shreeves (sshreeve@illinois.edu) on 2014-02-01T11:00:23Z Copyright 2011 Andrew Nieuwkoop Solid-state NMR protein structure determination fibrils GB1 alpha synuclein Parkinson’s disease TEDOR proton detection nuclear magnetic resonance (NMR) Structure determination of proteins and protein aggregates by magic-angle spinning solid-state NMR Dissertation / Thesis text Chemistry 1413 Chemistry 0335 University of Illinois at Urbana-Champaign Dissertation Ph.D. PHD:Chemistry -UIUC 10KS0335PHD