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What is the size range of particles in a colloid more than 1000 nm or between 1 nm and 1000 nm or between 100 nm and 1000 nm or between 1 nm and 10 nm?
Between 1 nanometre and 1 micrometre (= 1000 nm).
What is 0.185 nm in standard form?
1.85 x 10^-1 nm
What is 0278 nm in m?
0.278 nm = 0.000278 µm
How many nm is 400 km?
400 km = 4*1014 nm
If AB equals 3x plus 5 and NM equals 2x plus 1 then NM equals what?
NM equals 2x + 1, as stated in the question!
How to calculate protein concentration from absorbance at 280 nm?
To calculate protein concentration from absorbance at 280 nm, you can use the Beer-Lambert Law. This law states that absorbance is directly proportional to concentration and path length. By measuring the absorbance of the protein sample at 280 nm and using the extinction coefficient of the protein, you can calculate the concentration of the protein in the sample.
Which pair of amino acid will have the highest absorbance at 280 nm?
Aromatic amino acids such as tryptophan and tyrosine will have the highest absorbance at 280 nm due to their aromatic ring structures. These amino acids have strong UV absorbance properties and are commonly used in protein quantification assays due to their unique spectral properties at 280 nm.
How do you calculate the protein extinction coefficient for a given protein sample?
To calculate the protein extinction coefficient for a given protein sample, you can use the formula: Extinction coefficient (Absorbance at 280 nm) / (Concentration of protein in mg/ml). The absorbance at 280 nm can be measured using a spectrophotometer, and the concentration of the protein can be determined using methods such as the Bradford assay or the bicinchoninic acid (BCA) assay.
How can the protein absorbance at 280 nm be measured accurately?
The protein absorbance at 280 nm can be accurately measured using a spectrophotometer. This device measures the amount of light absorbed by the protein sample at that specific wavelength, providing a quantitative measurement of protein concentration. It is important to use a clean cuvette, prepare a proper protein sample, and calibrate the spectrophotometer before taking measurements to ensure accuracy.
Why does protein have an absorbance peak at 280nm?
Proteins have aromatic amino acids like tryptophan, tyrosine, and phenylalanine that absorb light at 280nm due to their aromatic rings. This absorbance peak at 280nm can be used to quantify the protein concentration in a sample, known as the A280 method.
What wavelength is the peak absorbance for cobalt chloride?
The peak absorbance for cobalt chloride typically occurs around 550-600 nm.
Why absorbance should be taken in 750 nm in lowrys method?
Absorbance at 750 nm in Lowry's method is used because it corresponds to the peak absorbance of the copper-tyrosine complex formed during the reaction, ensuring accurate measurement of the protein concentration. This wavelength specifically targets the color change associated with the biuret reaction, enhancing the sensitivity and specificity of the assay.
Why is the total protein are measured at 595 nm in the Bio-Rad assay?
The Bio-Rad protein assay measures the total protein content in a sample at 595 nm because this wavelength corresponds to the absorption peak of protein-bound Coomassie Brilliant Blue dye. When proteins are present in the sample, they bind to the dye, causing a shift in absorbance at 595 nm, which is used to accurately quantify the protein concentration.
Why do proteins absorb light at 280 nm?
Proteins absorb light at 280 nm because of the presence of aromatic amino acids, such as tryptophan and tyrosine, which have strong absorbance at this wavelength due to their unique chemical structures.
What wavelength is the peak absorbance of cobalt chloride?
The peak absorbance of cobalt chloride typically occurs at a wavelength around 550-600 nm. This range falls within the green to yellow-green region of the visible spectrum, where cobalt chloride absorbs light most strongly.
How can one calculate the extinction coefficient of a protein?
To calculate the extinction coefficient of a protein, you can use the formula: Extinction coefficient (A11cm) / (number of amino acids x molecular weight). A11cm is the absorbance at 280 nm for a 1 cm path length. This value can be determined experimentally using a spectrophotometer.
Why is the wavelength 275 nm used to measure absorbance of caffeine?
The wavelength of 275 nm is used to measure absorbance of caffeine because it corresponds to the maximum absorbance peak for caffeine. By using a wavelength where caffeine absorbs strongly, we can accurately measure its concentration in a sample based on the amount of light absorbed at 275 nm.
