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  Myelin basic protein - diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Harauz, G., Ishiyama, N., Hill, C. M. D., Bates, I. R., Libich, D. S., & Fares, C. (2004). Myelin basic protein - diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis. Micron, 35(7), 503-542. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T9N-4CVX8CC-1-1T&_cdi=5119&_user=38661&_orig=browse&_coverDate=10%2F31%2F2004&_sk=999649992&view=c&wchp=dGLbVlW-zSkWb&md5=95f48b0f11a5ccf5492c1c77a9953626&ie=/sdarticle.pdf.

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 Creators:
Harauz, G., Author
Ishiyama, N., Author
Hill, C. M. D., Author
Bates, I. R., Author
Libich, D. S., Author
Fares, C.1, Author           
Affiliations:
1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: 2D crystals; actin; calmodulin; citrulline; crystallisation; deimination; electron crystallography; electron microscopy; electron paramagnetic resonance (EPR); ganglioside; golli; His-tag; intrinsically unstructured protein; magic angle spinning (MAS); MTS-SL (methanethiosulphonate spin label); multiple sclerosis; myelin basic protein; natively unfolded protein; nuclear magnetic resonance (NMR); phosphatidylinositol; protein-lipid interactions; recombinant proteins; site-directed mutagenesis; site-directed spin labelling (SDSL); solid-state NMR; solution NMR
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Language(s): eng - English
 Dates: 2004
 Publication Status: Issued
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 Rev. Type: Peer
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Title: Micron
Source Genre: Journal
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Pages: - Volume / Issue: 35 (7) Sequence Number: - Start / End Page: 503 - 542 Identifier: -