Solid‐State NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins-Reference-Cited by-同舟云学术

Solid‐State NMR H–N–(C)–H and H–N–C–C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins

Published:2017-09-05 Issue:19 Volume:18 Page:2697-2703
ISSN:1439-4235
Container-title:ChemPhysChem
language:en
Short-container-title:ChemPhysChem

Author:

Fraga Hugo¹²^ORCID,Arnaud Charles‐Adrien¹,Gauto Diego F.¹,Audin Maxime³,Kurauskas Vilius¹,Macek Pavel¹,Krichel Carsten¹,Guan Jia‐Ying¹,Boisbouvier Jerome¹,Sprangers Remco³⁴,Breyton Cécile¹,Schanda Paul¹^ORCID

Affiliation:

1. Univ. Grenoble Alpes, CEACNRS, Institute for Structural Biology (IBS) 71 avenue des martyrs 38044 Grenoble France

2. Departamento de BioquimicaFaculdade de Medicina da Universidade do Porto Porto Portugal

3. Max Planck Institute for Developmental Biology Spemannstrasse 35 72076 Tübingen Germany

4. Department of Biophysics IUniversity of Regensburg 93053 Regensburg Germany

Funder

H2020 European Research Council

Publisher

Wiley

Subject

Physical and Theoretical Chemistry,Atomic and Molecular Physics, and Optics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cphc.201700572

Reference36 articles.

1. Structure of fully protonated proteins by proton-detected magic-angle spinning NMR

2. Atomic model of the type III secretion system needle

3. Mechanisms of Proton Conduction and Gating in Influenza M2 Proton Channels from Solid-State NMR

4. Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer

5. Atomic-Resolution Three-Dimensional Structure of HET-s(218−289) Amyloid Fibrils by Solid-State NMR Spectroscopy

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