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These methods are applied to study avidin and streptavidin, the proteins used in biotechnologies in connection with the ability of these proteins to strongly bind a low molecular mass compound biotin.
In this paper, the methodology is illustrated by a sample simulation of high molecular mass compound growth in an environment (T, H, H2, naphthalene, and acenaphthylene concentrations) of a low-pressure laminar premixed benzene/oxygen/argon flame with an equivalence ratio of 1.8.
Solvent extracts of the glycerol-MSM liquid culture obtained from ST5 were subjected to direct infusion using the positive ESI MS in order to determine the accurate molecular mass (compound identity) for the solvent extracted biosurfactant compounds.
Solvent extracts of the glycerol-MSM liquid culture obtained from ST34 were subjected to direct infusion using positive mode ESI MS in order to determine the accurate molecular mass (compound identity) for the solvent extracted biosurfactant compounds.
Although there are limitations for these techniques, using HPLC avoids the main problems associated with the use of gas chromatography such as thermal stability of components, their high molecular mass, compound destruction, and polarity of the compound.
Although selenium in its low molecular mass compound forms of selenite, selenide, selenate and selenoamino acids are rather reactive compounds that could react with redox sensitive amino acids directly or at higher concentrations yield cell death, the biological effect of selenium, including cell signalling, differentiation, cell growth and survival, is still debated.
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Genetic engineering provides the means for generating recombinant antibodies exhibiting extremely high specificity for even small molecular mass compounds.
Volatiles organic compounds (VOCs) are low molecular mass compounds with high vapor pressure and low to medium water solubility that exist in the gaseous state at room temperature (Herrmann [2010]).
Significant amounts of low molecular mass compounds, xylobiose and trace amounts of xylose were liberated from birch wood xylan after 24 h (Lin et al. [1999]) using Thermomyces lanuginosus enzyme; however cellulase activity could contaminate this endo-β(1 → 4 -xylanase preparation (Subramaniyan and Prema [2002]) explaining the results obtained.
These compounds were identified by virtual screening of 90,000 low molecular mass compounds using computational docking programs with the solved crystal structure of EBNA1.
This last purification step does not affect the polypeptide pattern of the protein, but removes unidentified low molecular mass compounds that appear to interfere with the protein lectin activity (results not shown).
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