(Q57097193)

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Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment

scientific article published on 19 January 2011

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scholarly article

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20 January 2020

Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment (English)

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20 January 2020

transmembrane protein

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4

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20 January 2020

author name string

Ying Fan

1

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20 January 2020

Lichi Shi

2

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20 January 2020

Vladimir Ladizhansky

3

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20 January 2020

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19 January 2011

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20 January 2020

Journal of Biomolecular NMR

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20 January 2020

49

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20 January 2020

2

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20 January 2020

151-161

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20 January 2020

https://scigraph.springernature.com/pub.10.1007/s10858-011-9473-9

0 references

Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation.

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Structural basis of diversification of fungal retinal proteins probed by site-directed mutagenesis ofLeptosphaeriarhodopsin

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FTIR spectroscopy of the K photointermediate of Neurospora rhodopsin: structural changes of the retinal, protein, and water molecules after photoisomerization

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Measurement of dipolar couplings in a uniformly (13)C,(15)N-labeled membrane protein: distances between the Schiff base and aspartic acids in the active site of bacteriorhodopsin.

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Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.

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Structural basis of the interaction between chemokine stromal cell-derived factor-1/CXCL12 and its G-protein-coupled receptor CXCR4.

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Solid-state NMR investigation of the buried X-proline peptide bonds of bacteriorhodopsin.

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1 reference

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Identifiers

10.1007/S10858-011-9473-9

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21246256%20AND%20SRC:MED&resulttype=core&format=json

20 January 2020

1 reference

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20 January 2020

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