Contact

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Rasmus Linser
Professor at the Ludwig-Maximilians-Universität Munich, Head of a Guest Group at the Max Planck Institute for Biophysical Chemistry
Phone:+49 551 201-2214Fax:+49 551 201-2202
Email:rali@...

Curriculum Vitae

Group Website at the Ludwig-Maximilians-Universität in Munich

Rasmus Linser

  Solid-State NMR Spectroscopy

Figure 1. The amyoidogenic hydrophobin EAS (solution structure of the monomer in A), forming water-repellant layers on fungal spores, as seen by EM (B) and by solid-state NMR at 60 kHz MAS (C), together with a preliminary structural model (D). Zoom Image
Figure 1. The amyoidogenic hydrophobin EAS (solution structure of the monomer in A), forming water-repellant layers on fungal spores, as seen by EM (B) and by solid-state NMR at 60 kHz MAS (C), together with a preliminary structural model (D). [less]

Recent technological developments have made solid-state NMR a versatile tool for characterization of biomolecules. This applies in particular to structural assessment of solid proteins as well as a determination of their dynamics. Our group has a specific focus on membrane proteins and amyloidogenic proteins. Membrane proteins play an eminent role for recent basic research as well as for drug discovery and can be assessed in their lipidic environment. Amyloids occur in the course of neurodegenerative diseases as well as in a functional context in different kinds of organisms (see Figure 1).

Our solid-state group is just starting out with a new set of people (early 2014), and we are currently looking for skilled and ambitious researchers to join the team. The research environment is set up for high-impact solid-state NMR research and well renown for its excellence. Our hardware includes 850 MHz (WB), 800 MHz (NB), 600 MHz (WB with DNP), and 400 MHz (WB) Bruker spectrometers with a comprehensive selection of probes amenable for leading-edge experimental approaches like ultra-fast MAS. Excellent biochemical expertise is provided by the highly knowledgeable and experienced team of Dr. Stefan Becker. This setting is of major relevance to our scientific performance.

<p>Figure 2. 4D diagonal-free HNNH correlations of the micro-crystalline SH3 domain of chicken a-spectrin (A), the nature of the obtained restraints (B), and the structural picture obtained from sparse but highest-quality structural restraints (C).</p> Zoom Image

Figure 2. 4D diagonal-free HNNH correlations of the micro-crystalline SH3 domain of chicken a-spectrin (A), the nature of the obtained restraints (B), and the structural picture obtained from sparse but highest-quality structural restraints (C).

<p>Figure 3. Stereo-ILV (and alanine) labeling of a membrane-anchor fragment of a eukaryotic transcription factor in micelles.</p> Zoom Image

Figure 3. Stereo-ILV (and alanine) labeling of a membrane-anchor fragment of a eukaryotic transcription factor in micelles.

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Our experimental approaches will combine state-of-the-art technical equipment with newest strategies towards protein characterization. This involves proton detection upon fast MAS and sparse protonation levels,1,2 higher-dimensionality experimental schemes,3 and newest assignment strategies4 including Non-Uniform-Sampling techniques (see Figure 2). Preparative features employ newest approaches in combinatorial labeling (see Figure 3) and exploitation of paramagnetic effects.5 Even though we focus on solid-state techniques, we support our research by solution-NMR.

 

Publications mentioned in the text:

1) R. Linser, M. Dasari, U. Fink, P. Schmieder, J.-M. Lopez del Amo, S. Marcovic, M. Hiller, H. Oschkinat, D. Oesterheld, B. Reif: Proton detected solid state NMR of fibrillar and membrane proteins, Angew. Chem., Int. Ed., 50 (19), 4508–4512.;

Cover Picture, Angew. Chem. Int. Ed., 50 (19), 4237 (2011).

2) V. Morris, R. Linser, K. L. Wilde, A. P. Duff, M. Sunde, A. Kwan: Solid-state NMR study of fungal hydrophobin rodlets, a functional amyloid, reveals a well-ordered b-sheet core amidst structural heterogeneity, Angew. Chem. Int. Ed. 51 (50), 12621-12625 (2012).

3) R. Linser, B. Bardiaux, V. Higman, U. Fink, B. Reif: Structure calculation from highly unambiguous amide and methyl 1H-1H distance restraints for a micro-crystalline protein with MAS solid state NMR, J. Am. Chem. Soc., 133 (15), 5905–5912 (2011).

4) as in R. Linser: Backbone Assignment of Perdeuterated Proteins Using Long-Range H/C-Dipolar Transfers, J. Biomol. NMR, 52 (2), 151-158 (2012),
    and A. Mainz, T. Religa, R. Sprangers, R. Linser, L. E. Kay, B. Reif: Solution-state NMR Spectroscopy at 1 MDa and Beyond, Angew. Chem. Int. Ed., 52 (33), 8746-8751 (2013).

5) R. Linser, U. Fink, B. Reif: Probing Surface Accessibility of Proteins using Paramagnetic Relaxation in MAS solid-state NMR Spectroscopy, J. Am. Chem. Soc., 131 (38), 13703-13708 (2009).

 
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