Results 1 to 10 of about 673,332 (240)
Protein design is a key factor for subunit–subunit association [PDF]
Proceedings of the National Academy of Sciences, 1999 Fundamental questions about role of the quaternary structures are addressed by using a statistical mechanics off-lattice model of a dimer protein. The model, in spite of its simplicity, captures key features of the monomer–monomer interactions revealed by atomic force experiments.
C. CLEMENTI, P. CARLONI, MARITAN, AMOS
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Subunit interactions of the Go protein [PDF]
FEBS Letters, 1992 The monoclonal antibody, MONO, recognizes an epitope on the G protein αo‐subunit [van der Voorn et al., submitted] and readily immunoprecipitates heterotrimeric Go proteins from solubilized, crude bovine brain membranes, as well as from a purified bovine brain G protein preparation.
Trudi Hengeveld +2 more
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Journal of Biological Chemistry, 1995 Guanine nucleotide-binding protein beta and gamma subunits form a tightly bound complex that can only be separated by denaturation. Assembly of beta and gamma subunits is a complicated process. The beta 1 and gamma 2 subunits can be synthesized in vitro in rabbit reticulocyte lysate and then assembled into dimers, but beta 1 cannot form beta gamma ...
Denise J. Spring +4 more
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Subunit Exchange in Protein Complexes
Journal of Molecular Biology, 2018 Over the past 50 years, protein complexes have been studied with techniques such as X-ray crystallography and electron microscopy, generating images which although detailed are static and homogeneous. More recently, limited application of in vivo fluorescence and other techniques has revealed that many complexes previously thought stable and ...
Tusk, S, Delalez, N, Berry, R
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The Est3 protein is a subunit of yeast telomerase [PDF]
Current Biology, 2000 EST1, EST2, EST3 and TLC1 function in a single pathway for telomere replication in the yeast Saccharomyces cerevisiae [1] [2], as would be expected if these genes all encode components of the same complex. Est2p, the reverse transcriptase protein subunit, and TLC1, the templating RNA, are subunits of the catalytic core of yeast telomerase [3] [4] [5 ...
Sara K. Evans +3 more
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Protein synthesis by ribosomes with tethered subunits [PDF]
Nature, 2015 The ribosome is a ribonucleoprotein machine responsible for protein synthesis. In all kingdoms of life it is composed of two subunits, each built on its own ribosomal RNA (rRNA) scaffold. The independent but coordinated functions of the subunits, including their ability to associate at initiation, rotate during elongation, and dissociate after protein ...
Orelle, Cédric +5 more
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ISOLATION OF A PROTEIN SUBUNIT FROM MICROTUBULES [PDF]
The Journal of Cell Biology, 1967 Sea-urchin sperm tails (Strongylocentrotus purpuratus) were obtained by amputation in synthetic sea water and were purified by differential centrifugation. Most of the arms of the outer nine doublets and soluble matrix proteins were removed by this treatment. The central pairs of microtubules were dissolved by dialysis against EDTA at pH 7.5.
Edwin W. Taylor, M. L. Shelanski
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G protein subunit interactions
Journal of Biological Chemistry, 1989 Abstract Modification of bovine brain G proteins by an N-hydroxysuccinimide ester of biotin has been studied. In the presence of GDP, but in the absence of Mg2+, neither guanine nucleotide binding nor GTPase activity of the protein was altered by modification using less than 1.25 mM biotin derivative with 1 mg/ml G protein.
J D Hildebrandt +2 more
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Subunit counting in membrane-bound proteins [PDF]
Nature Methods, 2007 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.
Maximilian H. Ulbrich, Ehud Y. Isacoff
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Autoacylation of G Protein α Subunits [PDF]
Journal of Biological Chemistry, 1996 The palmitoylation or S-acylation of at least some G protein alpha subunits is a dynamic process that is regulated in vivo by the activation of associated receptors. Highly purified, myristoylated Gialpha1 and other G protein alpha subunits react spontaneously with palmitoyl-CoA in vitro to form thioesterified proteins.
Alfred G. Gilman, Joseph A. Duncan
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