Results 221 to 230 of about 912,209 (260)
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Subunit interactions of GTP‐binding proteins
European Journal of Biochemistry, 1992Fluorescence energy transfer [cf. Förster, T. (1948) Ann. Phys. 6, 55–75] was tested for its suitability to study quantitative interactions of subunits of Go with each other and these subunits or trimeric Go with the β1‐adrenoceptor in detergent micelles or after reconstitution into lipid vesicles [according to Feder, D., Im, M.‐J., Klein, H.
Heithier, H. +9 more
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G protein subunits in lung cells
Life Sciences, 1994Many hormones and neurotransmitters bind to membrane-bound receptors that are coupled to signal generating enzymes or ion channels via signal transducing GTP-binding proteins termed G proteins. Although receptors and second messengers have been extensively studied in cells of the respiratory system, the G proteins responsible for the coupling of these ...
C W, Emala +3 more
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Placental Proteins and Their Subunits as Tumor Markers
Annals of Internal Medicine, 1975Abstract Placental proteins and their unique subunits are not normally detected in the circulation, even with immunoassays sensitive to 1 ng/ml.
SAUL W. ROSEN +5 more
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EFFECTS OF DIMETHYL SULFOXIDE ON SUBUNIT PROTEINS*
Annals of the New York Academy of Sciences, 1975The effects of DMSO are thought to result from the formation of hydrogen bonds with proton-donor groups on biopolymers, which are stronger than those formed with water. Since DMSO contains methyl groups, however, effects on hydrophobic bonding in proteins could be expected at higher DMSO levels.
T R, Henderson +2 more
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2009
Protein dimers are common in catalysis and regulation. Their associations are either homodimers (identical monomers) or heterodimers (nonidentical monomers). The molecular principles of protein dimer interactions are difficult to understand mainly due to the geometrical and chemical characteristics of proteins.
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Protein dimers are common in catalysis and regulation. Their associations are either homodimers (identical monomers) or heterodimers (nonidentical monomers). The molecular principles of protein dimer interactions are difficult to understand mainly due to the geometrical and chemical characteristics of proteins.
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The protein subunit of calf brain neurofilament
Journal of Neurobiology, 1974AbstractA preparation of the protein subunits from calf neurofilaments has been obtained. Axon segments from an homogenate of calf brain white matter have been concentrated by a subcellular fractionation procedure. After further steps to achieve a complete elimination of unbound lipid, the neurofilament protein was dissolved in 4M guanidine ...
P F, Davison, B, Winslow
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An investigation of protein subunit and domain interfaces
"Protein Engineering, Design and Selection", 1988Protein structures were collected from the Brookhaven Database of tertiary architectures that displayed oligomeric association (24 molecules) or whose polypeptide folding revealed domains (34 proteins). The subunit and domain interfaces for these proteins were respectively examined from the following aspects: percentage water-accessible surface area ...
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Proteins of Rabbit Reticulocyte Ribosomal Subunits
Nature, 1970BY comparison with those of prokaryotic cells, especially Escherichia coli, little is known about the ribosornes of eukaryotes. The present analysis of ribosomal proteins from rabbit reticulocytes indicates that—in spite of the larger size of the particle and a higher protein content—the number of different proteins is not significantly greater than ...
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Dissociation of protein subunits by maleylation
Biochemical and Biophysical Research Communications, 1968C L, Sia, B L, Horecker
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