125IIodonaphtylazide labeling selectively a cysteine residue in the F0of the ATP-synthase fromE. coliis unsuitable for topographic studies of membrane proteins (Q72792205)

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scientific article published on August 22, 1983

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English	125IIodonaphtylazide labeling selectively a cysteine residue in the F0of the ATP-synthase fromE. coliis unsuitable for topographic studies of membrane proteins	scientific article published on August 22, 1983

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29 October 2019

125IIodonaphtylazide labeling selectively a cysteine residue in the F0of the ATP-synthase fromE. coliis unsuitable for topographic studies of membrane proteins (English)

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1 September 2023

125IIodonaphtylazide labeling selectively a cysteine residue in the F0 of the ATP-synthase from E. coli is unsuitable for topographic studies of membrane proteins (English)

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1 September 2023

membrane protein

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Escherichia coli

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1 September 2023

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1 September 2023

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10.1016/0014-5793(83)80974-0

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1 September 2023

structural biology

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1 September 2023

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author name string

J. Hoppe

1

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1 September 2023

P. Friedl

2

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1 September 2023

B. B. Jørgensen

3

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1 September 2023

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1 September 2023

publication date

1 August 1983

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29 October 2019

22 August 1983

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National Center for Biotechnology Information

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1 September 2023

number of pages

4

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1 September 2023

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http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(83)80974-0/fullpdf

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1 September 2023

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29 October 2019

160

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29 October 2019

1-2

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29 October 2019

239-242

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29 October 2019

Photoaffinity labeling

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Photoaffinity Labeling of Biological Systems

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New approach to the study of phospholipid-protein interactions in biological membranes. Synthesis of fatty acids and phospholipids containing photosensitive groups

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5-[125I]Iodonaphthyl azide, a reagent to determine the penetration of proteins into the lipid bilayer of biological membranes

1 reference

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Photogenerated reagents for membrane labeling. 2. Phenylcarbene and adamantylidene formed within the lipid bilayer

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Photoreactive labeling of M13 coat protein in model membranes by use of a glycolipid probe

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Labelling of the intramembranous region of the major sialoglycoprotein of human erythrocytes with a photosensitive hydrophobic probe

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Photolabelling of membrane proteins with photoactive phospholipids

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Selective labeling of the hydrophobic core of membranes with 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine, a carbene-generating reagent.

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The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit δ of the membrane bound ATP synthase of Escherichia coli

1 reference

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Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from : Prediction of the primary structure of F0 subunits

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The atp operon: nucleotide sequence of the promoter and the genes for the membrane proteins, and the delta subunit of Escherichia coli ATP-synthase

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The proteolipid of a mutant ATPase from Escherichia coli defective in H+-conduction contains a glycine instead of the carbodiimide-reactive aspartyl residue

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Identification of Amino-Acid Substitutions in the Proteolipid Subunit of the ATP Synthase from Dicyclohexylcarbodiimide-Resistant Mutants of Escherichia coli

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The ATP Synthetase of Escherichia coli K12: Purification of the Enzyme and Reconstitution of Energy-Transducing Activities

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Amino acid sequence of the proteolipid subunit of the proton-translocating ATPase complex from the thermophilic bacterium PS-3.

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10.1016/0014-5793(83)80974-0

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6224703%20AND%20SRC:MED&resulttype=core&format=json

29 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6224703%20AND%20SRC:MED&resulttype=core&format=json

29 October 2019

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