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  Dynamics in the solid-state: Perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes.

Linser, R., Sarkar, R., Krushelnitzky, A., Mainz, A., & Reif, B. (2014). Dynamics in the solid-state: Perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes. Journal of Biomolecular NMR, 59(1), 1-14. doi:10.1007/s10858-014-9822-6.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0018-9F0C-C Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-DF6D-C
Genre: Journal Article

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1977443.pdf (Publisher version), 3MB
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http://link.springer.com/content/pdf/10.1007%2Fs10858-014-9822-6.pdf (Publisher version)
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 Creators:
Linser, R.1, Author           
Sarkar, R., Author
Krushelnitzky, A., Author
Mainz, A., Author
Reif, B., Author
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1Research Group of Solid-State NMR-2, MPI for Biophysical Chemistry, Max Planck Society, ou_1950286              

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Free keywords: MAS solid-state NMR; Protein dynamics; Amyloid fibrils: Membrane proteins; Soluble protein complexes
 Abstract: Aggregates formed by amyloidogenic peptides and proteins and reconstituted membrane protein preparations differ significantly in terms of the spectral quality that they display in solid-state NMR experiments. Structural heterogeneity and dynamics can both in principle account for that observation. This perspectives article aims to point out challenges and limitations, but also potential opportunities in the investigation of these systems.

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Language(s): eng - English
 Dates: 2014-03-052014
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1007/s10858-014-9822-6
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Title: Journal of Biomolecular NMR
Source Genre: Journal
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Pages: - Volume / Issue: 59 (1) Sequence Number: - Start / End Page: 1 - 14 Identifier: -