Results 251 to 260 of about 295,838 (293)
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Soft Matter, 2014
We report the synthesis and properties of a dibenzophenazine discotic dimer, which was found to adopt a folded conformation in solution. This stable π-stacked structure persists at elevated temperatures and in all solvents examined. Folding allows the dimer to assemble into a columnar liquid crystal phase, despite its short linking group.
Kevin J A, Bozek, Vance E, Williams
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We report the synthesis and properties of a dibenzophenazine discotic dimer, which was found to adopt a folded conformation in solution. This stable π-stacked structure persists at elevated temperatures and in all solvents examined. Folding allows the dimer to assemble into a columnar liquid crystal phase, despite its short linking group.
Kevin J A, Bozek, Vance E, Williams
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Journal of Molecular Spectroscopy, 1999
Spectra of the symmetric nu1 vibration of the NO dimer have been recorded in gas phase at low temperature, with a high-resolution infrared Fourier transform spectrometer. All the lines were least-squares fitted to a Voigt profile convoluted with the well-known apparatus function of the spectrometer. By means of this method, the frequencies of more than
, Dkhissi, , Lacome, , Perrin
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Spectra of the symmetric nu1 vibration of the NO dimer have been recorded in gas phase at low temperature, with a high-resolution infrared Fourier transform spectrometer. All the lines were least-squares fitted to a Voigt profile convoluted with the well-known apparatus function of the spectrometer. By means of this method, the frequencies of more than
, Dkhissi, , Lacome, , Perrin
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2012
The specific self-association of proteins to form homodimers and higher order oligomers is an extremely common event in biological systems. In this chapter we review the prevalence of protein oligomerization and discuss the likely origins of this phenomenon.
Jacqueline M, Matthews, Margaret, Sunde
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The specific self-association of proteins to form homodimers and higher order oligomers is an extremely common event in biological systems. In this chapter we review the prevalence of protein oligomerization and discuss the likely origins of this phenomenon.
Jacqueline M, Matthews, Margaret, Sunde
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2008
Tropomyosins consist of nearly 100% alpha-helix and assemble into paralleldimeric coiled-coils. Nonmusde as well as muscle tropomyosins can form homodimers, however, expression of both muscle alpha and beta tropomyosin subunits results in the preferential formation of stable alpha/beta heterodimers in native muscle.
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Tropomyosins consist of nearly 100% alpha-helix and assemble into paralleldimeric coiled-coils. Nonmusde as well as muscle tropomyosins can form homodimers, however, expression of both muscle alpha and beta tropomyosin subunits results in the preferential formation of stable alpha/beta heterodimers in native muscle.
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Journal of Statistical Physics
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zbMATH Open Web Interface contents unavailable due to conflicting licenses.
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Dimerization of retroviral RNA genomes: an inseparable pair
Nature Reviews Microbiology, 2004jean-christophe Paillart +2 more
exaly
KRAS Dimerization Impacts MEK Inhibitor Sensitivity and Oncogenic Activity of Mutant KRAS
Cell, 2018Chiara Ambrogio +2 more
exaly
Ligand-Induced, Receptor-Mediated Dimerization and Activation of EGF Receptor
Cell, 2002Joseph Schlessinger
exaly