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View All Magnetic Resonance Techniques at Instruct
View All Solid State NMR at Instruct
CERM/CIRMMP offers unique research capabilities in the field of solid-state NMR of biomolecules by providing state of the art instrumentation and expertise to perform, at the highest level, the most comprehensive array of experiments needed for the structure and dynamic characterisation of biological macromolecules and their complexes.
Solid-state NMR available at CERM/CIRMMP can be used to obtain atomic-level structural information of biomolecules when they are forming aggregates (e.g.: fibrils), or when they are bound to or trapped in solid matrices that lack long-range three-dimensional order (e.g.: immobilized enzymes), or even for those systems that are too large and escape the conventional limits of NMR in solution.
The infrastructure includes high and ultra-high field spectrometers equipped with CP MAS probes for solid-state NMR measurements, ranging from 4 mm to 0.7 mm and reaching MAS speed up to 111 kHz, that allow to support a wide range of scientific applications. In particular, the Bruker Avance NEO 1200 MHz standard-bore system is equipped with 0.7 mm CP MAS 1H/13C/15N for biomolecular applications; the Bruker Avance III 850 MHz wide-bore system is equipped with 3.2 mm CP MAS DVT 15N/13C/1H, 1.3 mm CP MAS 1H19F/BB/15N and 0.7 mm CP MAS 1H/13C/15N for materials and biomolecular applications; the Bruker Avance III 800 MHz standard-bore system is equipped with 3.2 mm CP MAS DVT E-free 15N/13C/1H that allow to perform measurements on inorganic materials and biomaterials with high salt concentrations, 1.3 mm 3γ 1H19F/BB-X/BB-Y for hetero-nuclear detection, and 1.3 mm CP MAS 1H/13C/15N probes for biomolecular applications; the Bruker Avance NEO 700 MHz system comes with two CP MAS BB/BB/1H probe-heads (4- and 3.2 mm) which allow to record also solid-state NMR spectra on 27Al and 11B nuclei.
Expertise described below is not exhaustive and experiments can be adapted, and expanded on the basis of the user needs.
Structural and dynamic behavior determination
Excellent instrumentation and expertise are available to users for acquiring all the conventional experiments required for the structural and dynamic characterization of biological macromolecules and their complexes in the solid-state.
Structural characterization of metalloproteins and paramagnetic systems
Analysis of paramagnetic proteins at the solid-state is a long-lasting expertise at CERM/CIRMMP, where the first structural characterization of a paramagnetic metalloprotein (MMP12), relying uniquely on solid-state NMR restraints, was achieved.
Structural determination of amyloid fibrils
CERM/CIRMMP infrastructure provides state-of-the-art instrumentation and expertise to perform the most comprehensive array of experiments needed for the structural characterization of amyloid fibrils using the 13C-detection approach.
High Order Structure (HOS) determination
HOS can provide information on the safety and efficacy of protein therapeutics. NMR spectroscopy is a highly reliable and precise technique for effectively assessing this important structural characteristic. Our high-field instruments for both solution and solid-state NMR, combined with our extensive expertise in characterizing biologics, enable to offer comprehensive analysis and support for the application of this approach. An indirect information about the HOS of a biologics can be also achieved by looking at its interaction with the target.
Characterization of biomaterials
Detailed structural insights can be obtained for proteins encapsulated in or adsorbed onto materials. Moreover, ligand interactions with the encapsulated proteins can also be monitored thanks to the high resolution spectrometers available.
Structural characterization of inorganic and organic materials
The available instrumentation supports solid-state NMR measurements on a wide range of nuclei, enabling detailed characterization of chemical interactions within inorganic and organic materials.
Solid State NMR spectroscopy measurements can be performed on virtually any typeof biological solid. CERM/CIRMMP has experience of working with several different kinds of biosolids including microcrystalline proteins, amyloids, fibrils, biomaterials and sedimented solutes.
To obtain structural information on proteins by solid- state NMR, 15N/13C isotopically labelled samples are usually required. Deuteration may also be necessary when using 1.3 mm rotors to perform 1H-detected experiments.
Thanks to recent upgrades, our 1.2 GHz spectrometer is now equipped with a 0.7 mm solid state MAS Probe. Ultra-fast magic angle spinning at 1.2 GHz allows to record high quality 1H-detected spectra with outstanding resolution, without the need of deuteration, enabling to monitor dynamics and interaction at the solid-state. Users can thus perform the following studies: assignment, determination of structural constraints; local dynamics; protein-protein and protein-ligand interaction; determination of paramagnetic effects.
The support might include instruments setup, data acquisition and data analysis. Assistance and supervision will be assigned based on the expertise of the visiting scientist.
In case of remote access, the transfer to the rotor is performed by our staff only for 3.2- and 4-mm rotors and non-air/light sensitive samples. For high MAS frequencies (rotors of 1.3 mm or 0.7 mm), samples must be provided directly in the rotor, after testing that they spin properly.
The visiting scientist must communicate the scientific plan of the experiments and the contacts to arrange the visit. On average a visit is one week of instrument time and it can be arranged as a physical visit to the facility or by mailing-in the samples. Some projects might require more time, up to several weeks, depending on the complexity of the work to be performed and the experience of the visiting scientist in the field.
Contact the facility staff before submitting your proposal, so that the access request is in agreement with the scientific plan of the experiments.
