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Agincourt can run up to 140,000 crystallisation experiments at once to find the best conditions for coaxing a sample of protein to form crystals.Meanwhile, imaging devices which take digital snapshots four times a second work out when the sample is ready.
The prepared sample of protein layer was stored in PBS at 4 °C before use.
Finally, the prepared sample of protein layer was kept in PBS at 4°C until use.
The sample of protein concentrate was dissolved in 6 mL of 6 N HCl and was subjected to hydrolysis in boiling water bath for a period of 24 h.
Concentrated ligand solutions in Buffer B were titrated into a 400 µl sample of protein (180 nM in Buffer B) and Trp fluorescence monitored.
An 800 µg sample of protein A coupled to Sepharose (Sigma-Aldrich, USA) was incubated with 2.8 mg of complete proteins obtained from peptide-immunized rabbit serum, in PBS solvent in a final volume of 130 µl.
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Fundamentally, every existing sample of proteins is subject to these problems.
Again, we normalized the intensities of actin and myosin in each subject sample against a common reference sample of proteins derived from exfoliated cells in a saliva sample from pooled healthy donors.
One mg per sample of proteins was immunoprecipitated using 2 µg of anti-E5 antibody (kindly provided by Dr. Campo, Glasgow University, Scotland) and 30 µl of G-sepharose (Ge Healthcare).
Distillation was performed by using a 225 μL sample of protein-free serum to which was added a 25 μL internal standard solution consisting of 1.25 mM valeric acid and 1.06 M formic acid.
Finally, we propose three diagnostic statistics to indicate the degree to which (a) hitch-hiking of deleterious mutations (b) background selection and (c) clonal interference affect a sample of protein-coding sequences.
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