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Literature DB >> 24595988

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

Rasmus Linser¹, Riddhiman Sarkar, Alexey Krushelnitzky, Andi Mainz, Bernd Reif.

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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Year: 2014 PMID： 24595988 DOI： 10.1007/s10858-014-9822-6

Source DB: PubMed Journal: J Biomol NMR ISSN： 0925-2738 Impact factor: 2.835

110 in total

1. Accurate calculation of the density of proteins.

Authors: M L Quillin; B W Matthews
Journal: Acta Crystallogr D Biol Crystallogr Date: 2000-07

2. Characterization of membrane proteins in isolated native cellular membranes by dynamic nuclear polarization solid-state NMR spectroscopy without purification and reconstitution.

Authors: Tomas Jacso; W Trent Franks; Honor Rose; Uwe Fink; Jana Broecker; Sandro Keller; Hartmut Oschkinat; Bernd Reif
Journal: Angew Chem Int Ed Engl Date: 2011-11-23 Impact factor: 15.336

3. Solid-state protein-structure determination with proton-detected triple-resonance 3D magic-angle-spinning NMR spectroscopy.

Authors: Donghua H Zhou; John J Shea; Andrew J Nieuwkoop; W Trent Franks; Benjamin J Wylie; Charles Mullen; Dennis Sandoz; Chad M Rienstra
Journal: Angew Chem Int Ed Engl Date: 2007 Impact factor: 15.336

4. Quantitative measurement of differential 15N-H(alpha/beta)T2 relaxation rates in a perdeuterated protein by MAS solid-state NMR spectroscopy.

Authors: Veniamin Chevelkov; Anne Diehl; Bernd Reif
Journal: Magn Reson Chem Date: 2007-12 Impact factor: 2.447

5. Optimum levels of exchangeable protons in perdeuterated proteins for proton detection in MAS solid-state NMR spectroscopy.

Authors: Umit Akbey; Sascha Lange; W Trent Franks; Rasmus Linser; Kristina Rehbein; Anne Diehl; Barth-Jan van Rossum; Bernd Reif; Hartmut Oschkinat
Journal: J Biomol NMR Date: 2009-08-22 Impact factor: 2.835

6. Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion.

Authors: Paul Schanda; Matthias Huber; Jérôme Boisbouvier; Beat H Meier; Matthias Ernst
Journal: Angew Chem Int Ed Engl Date: 2011-09-14 Impact factor: 15.336

7. Proton-detected solid-state NMR reveals intramembrane polar networks in a seven-helical transmembrane protein proteorhodopsin.

Authors: Meaghan E Ward; Lichi Shi; Evelyn Lake; Sridevi Krishnamurthy; Howard Hutchins; Leonid S Brown; Vladimir Ladizhansky
Journal: J Am Chem Soc Date: 2011-10-07 Impact factor: 15.419

8. Dynamics of reassembled thioredoxin studied by magic angle spinning NMR: snapshots from different time scales.

Authors: Jun Yang; Maria Luisa Tasayco; Tatyana Polenova
Journal: J Am Chem Soc Date: 2009-09-30 Impact factor: 15.419

9. Functional amyloid formation within mammalian tissue.

Authors: Douglas M Fowler; Atanas V Koulov; Christelle Alory-Jost; Michael S Marks; William E Balch; Jeffery W Kelly
Journal: PLoS Biol Date: 2006-01 Impact factor: 8.029

10. Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy.

Authors: Martin Tollinger; Astrid C Sivertsen; Beat H Meier; Matthias Ernst; Paul Schanda
Journal: J Am Chem Soc Date: 2012-08-28 Impact factor: 15.419

18 in total

Review 1. Basic experiments in ²H static NMR for the characterization of protein side-chain dynamics.

Authors: Liliya Vugmeyster; Dmitry Ostrovsky
Journal: Methods Date: 2018-04-27 Impact factor: 3.608

2. Ultrafast Hydrogen-Bonding Dynamics in Amyloid Fibrils.

Authors: Ileana M Pazos; Jianqiang Ma; Debopreeti Mukherjee; Feng Gai
Journal: J Phys Chem B Date: 2018-06-21 Impact factor: 2.991

3. Comparative Dynamics of Methionine Side-Chain in FMOC-Methionine and in Amyloid Fibrils.

Authors: Liliya Vugmeyster; Dmitry Ostrovsky
Journal: Chem Phys Lett Date: 2017-02-14 Impact factor: 2.328

4. Protein dynamics in the solid state from 2H NMR line shape analysis: a consistent perspective.

Authors: Eva Meirovitch; Zhichun Liang; Jack H Freed
Journal: J Phys Chem B Date: 2015-02-03 Impact factor: 2.991

5. Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils.

Authors: Dan Fai Au; Dmitry Ostrovsky; Riqiang Fu; Liliya Vugmeyster
Journal: J Biol Chem Date: 2019-02-08 Impact factor: 5.157

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

1. Accurate calculation of the density of proteins.

2. Characterization of membrane proteins in isolated native cellular membranes by dynamic nuclear polarization solid-state NMR spectroscopy without purification and reconstitution.

3. Solid-state protein-structure determination with proton-detected triple-resonance 3D magic-angle-spinning NMR spectroscopy.

4. Quantitative measurement of differential 15N-H(alpha/beta)T2 relaxation rates in a perdeuterated protein by MAS solid-state NMR spectroscopy.

5. Optimum levels of exchangeable protons in perdeuterated proteins for proton detection in MAS solid-state NMR spectroscopy.

6. Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion.

7. Proton-detected solid-state NMR reveals intramembrane polar networks in a seven-helical transmembrane protein proteorhodopsin.

8. Dynamics of reassembled thioredoxin studied by magic angle spinning NMR: snapshots from different time scales.

9. Functional amyloid formation within mammalian tissue.

10. Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy.

Review 1. Basic experiments in ²H static NMR for the characterization of protein side-chain dynamics.

2. Ultrafast Hydrogen-Bonding Dynamics in Amyloid Fibrils.

3. Comparative Dynamics of Methionine Side-Chain in FMOC-Methionine and in Amyloid Fibrils.

4. Protein dynamics in the solid state from 2H NMR line shape analysis: a consistent perspective.

5. Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils.

6. Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.

7. Flexibility and Solvation of Amyloid-β Hydrophobic Core.

Review 8. Static solid-state ²H NMR methods in studies of protein side-chain dynamics.

9. Effect of Post-Translational Modifications and Mutations on Amyloid-β Fibrils Dynamics at N Terminus.

10. Peptide and Protein Dynamics and Low-Temperature/DNP Magic Angle Spinning NMR.

Review 1. Basic experiments in 2H static NMR for the characterization of protein side-chain dynamics.

Review 8. Static solid-state 2H NMR methods in studies of protein side-chain dynamics.

Review 1. Basic experiments in ²H static NMR for the characterization of protein side-chain dynamics.

Review 8. Static solid-state ²H NMR methods in studies of protein side-chain dynamics.