Protein NMR Spectroscopy at 150 kHz Magic‐Angle Spinning Continues To Improve Resolution and Mass Sensitivity-Reference-Cited by-同舟云学术

Protein NMR Spectroscopy at 150 kHz Magic‐Angle Spinning Continues To Improve Resolution and Mass Sensitivity

Published:2020-07-29 Issue:17 Volume:21 Page:2540-2548
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Schledorn Maarten¹,Malär Alexander A.¹,Torosyan Anahit¹,Penzel Susanne¹,Klose Daniel¹,Oss Andres²,Org Mai‐Liis²,Wang Shishan³,Lecoq Lauriane³,Cadalbert Riccardo¹,Samoson Ago²,Böckmann Anja³,Meier Beat H.¹^ORCID

Affiliation:

1. Physical ChemistryETH Zürich 8093 Zürich Switzerland

2. Institute of Health TechnologiesTallinn University of Technology Akadeemia tee 15a 12618 Tallinn Estonia

3. Institut de Biologie et Chimie des Protéines MMSB UMR 5086 CNRS/Université de Lyon, Labex Ecofect 7 passage du Vercors 69367 Lyon France

Funder

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.202000341

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2. Atomic‐Resolution Three‐Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation

3. Die atomare dreidimensionale Struktur von Amyloid‐β‐Fibrillen mit der Osaka‐Mutation

4. Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

5. Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

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