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To determine the absorbance at 320 nm, you need to measure the light intensity before and after it passes through a sample at that wavelength. Absorbance (A) is calculated using the formula A = log10(I0/I), where I0 is the incident light intensity and I is the transmitted light intensity. The specific absorbance value will depend on the properties of the sample being tested. If you have a specific sample or context in mind, please provide more details for a more tailored response.

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What is maximum absorbance of methyle orange at 242 nm?

The maximum absorbance of methyl orange typically occurs at around 464 nm, not 242 nm. At 242 nm, the absorbance may be lower or not significant, as this wavelength is outside the main absorption range for methyl orange. For accurate absorbance values, it is important to refer to specific absorption spectra or experimental data for methyl orange.


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.


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The lambda max (λmax) for metronidazole is typically around 318-320 nm when measured in a UV-Vis spectrophotometer. This is the wavelength at which metronidazole shows maximum absorbance.


What is the specific absorbance of hypericin?

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What wavelength is the peak absorbance for cobalt chloride?

The peak absorbance for cobalt chloride typically occurs around 550-600 nm.


What is the maximum absorbance for beta-carotene?

The maximum absorbance for beta-carotene is around 450-480 nm. This range corresponds to the absorption of light in the visible spectrum by beta-carotene molecules.


Why do protein have 2 absorbance peak at 280 nm?

Proteins exhibit two absorbance peaks around 280 nm primarily due to the presence of aromatic amino acids, such as tryptophan and tyrosine. Tryptophan has a strong absorbance peak near 280 nm, while tyrosine contributes a smaller peak at the same wavelength. The combined absorbance from these amino acids allows for the estimation of protein concentration in solutions, as they are key components in the protein structure.


What is the significance of NADH absorbance at 340 nm in biochemical assays?

The absorbance of NADH at 340 nm is significant in biochemical assays because it can be used to measure the activity of enzymes that utilize NADH as a cofactor. By monitoring the changes in absorbance at 340 nm, researchers can track the conversion of NADH to its oxidized form, NAD, which provides valuable information about enzyme kinetics and metabolic processes.


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What is the absorbance value for tartrazine?

The absorbance value for tartrazine will depend on the specific wavelength at which it is measured. Tartrazine typically absorbs light most strongly in the visible spectrum, around 425-430 nm. To determine the exact absorbance value, you would need to measure the absorbance of a known concentration of tartrazine at this wavelength using a spectrophotometer.


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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.


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.