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Analysis of the organic solvent effect on the structure of dehydrated proteins by isothermal calorimetry, differential scanning calorimetry and FTIR spectroscopy proteins in anhydrous organic solvents in the temperature range 60-105 °C. This means that dehydrated

High-level expression of the monomeric SARS-CoV-2 S protein RBD 320-537 in stably transfected CHO cells by the EEF1A1-based plasmid vectorThe spike (S) protein is one of the three proteins forming the coronaviruses’ viral envelope

A study of the hydration of ribonuclease A using densitometry: Effect of the protein hydrophobicity and polarity function of composition at 25 °C. The excess quantities for RNase A were compared with the published data

Effects of abscisic acid, low temperature, and plant age on cytoskeleton and phosphorylated proteins of tubulin, actin, and phosphorylated proteins and the structural organization of microtubules (MTs) in cells

Effects of abscisic acid, low temperature, and plant age on cytoskeleton and phosphorylated proteins acclimation of plants (3°C, 7 days) did not change the level of tubulin and actin proteins, it evoked

NMR assignments of the WBSCR27 protein related to Williams-Beuren syndrome by hemizygous deletion of several genes in chromosome 7. One of the removed genes encodes the WBSCR27 protein

The Temperature-Dependent Selectivity of Potential Interaction Partners for the Small Heat Shock Protein IbpA from Acholeplasma laidlawii significantly differed between the protein pool co-eluting with IbpA under cooling (4 °C) and the entire

SKP2 attenuates autophagy through Beclin1-ubiquitination and its inhibition reduces MERS-Coronavirus infection1 (BECN1) is one of its key regulators. Here, we identified S-phase kinase-associated protein 2 (SKP

Effect of abscisic acid and cold acclimation on the cytoskeletal and phosphorylated proteins in different cultivars of Triticum aestivum L.In winter wheat, the tubulin and 60 kDa-phosphorylated proteins/actin ratio is considerably higher

Experimental Approach to Study the Effect of Mutations on the Protein Folding PathwayIs it possible to compare the physicochemical properties of a wild-type protein and its mutant form

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