NMR “Crystallography” for Uniformly ( 13 C, 15 N)‐Labeled Oriented Membrane Proteins-Reference-Cited by-同舟云学术

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NMR “Crystallography” for Uniformly ( 13 C, 15 N)‐Labeled Oriented Membrane Proteins

Published:2020-01-23 Issue:9 Volume:59 Page:3554-3557
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Awosanya Emmanuel O.¹,Lapin Joel¹,Nevzorov Alexander A.¹^ORCID

Affiliation:

1. Department of Chemistry North Carolina State University 2620 Yarbrough Drive Raleigh NC 27695-8204 USA

Funder

Division of Molecular and Cellular Biosciences

Army Research Office

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.201915110

Reference52 articles.

1. MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles

2. Understanding peptide interactions with the lipid bilayer: a guide to membrane protein engineering

3. Lipid–protein interactions

4. Membrane proteins bind lipids selectively to modulate their structure and function

5. PIP2 regulates psychostimulant behaviors through its interaction with a membrane protein

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Hybridizing isotropic and anisotropic solid-state NMR restraints for membrane protein structure determination;Solid-State NMR;2020-12

2. Computer-generated pulse sequences for 1H-15N and 1Hα-13Cα separated local-field experiments;Journal of Magnetic Resonance;2020-08

3. Polymorphic Forms of Valinomycin Investigated by NMR Crystallography;International Journal of Molecular Sciences;2020-07-11

4. Monitoring the Site-Specific Solid-State NMR Data in Oligopeptides;International Journal of Molecular Sciences;2020-04-13

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