Subunit counting in membrane-bound proteins
Copyright policy )Subunit counting in membrane-bound proteins
The subunit number and stoichiometry of membrane-bound proteins are difficult to determine without disrupting their membrane environment. Here we describe a single-molecule technique for counting subunits of proteins in live cell membranes by observing bleaching steps of GFP fused to a protein of interest. After testing the method with proteins of known stoichiometry expressed in Xenopus laevis oocytes, we resolved the composition of NMDA receptors composed of NR1 and NR3 subunits.
- University of California, Berkeley United States
- Lawrence Berkeley National Laboratory United States
Recombinant Fusion Proteins, Green Fluorescent Proteins, Cyclic Nucleotide-Gated Cation Channels, Membrane Proteins, Receptors, N-Methyl-D-Aspartate, Ion Channels, Protein Subunits, Xenopus laevis, Oocytes, Animals, Calcium Channels, Cloning, Molecular, Cells, Cultured
Recombinant Fusion Proteins, Green Fluorescent Proteins, Cyclic Nucleotide-Gated Cation Channels, Membrane Proteins, Receptors, N-Methyl-D-Aspartate, Ion Channels, Protein Subunits, Xenopus laevis, Oocytes, Animals, Calcium Channels, Cloning, Molecular, Cells, Cultured
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).627 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 0.1% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 1% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 1%
Citations provided by BIP!Popularity provided by BIP!