Podcast
Questions and Answers
What is the primary purpose of fluorescence spectroscopy?
What is the primary purpose of fluorescence spectroscopy?
- To separate molecules based on charge in an electric field
- To measure the size of molecules based on their fluorescence
- To excite electrons in a sample with light and measure lower energy light emission (correct)
- To denature proteins and run them in a gel
Which characteristic is associated with fluorescent molecules?
Which characteristic is associated with fluorescent molecules?
- Highly conjugated systems, many rings, and rigid and planar structure (correct)
- Small size and random orientation
- Large molecular weight and irregular shape
- Low energy levels and flexible structure
What is the Stoke shift in fluorescence spectroscopy?
What is the Stoke shift in fluorescence spectroscopy?
- The interference caused by the light source and prism
- The difference between excitation and emission wavelengths (correct)
- The measure of energy transfer in the sample
- The sensitivity of the fluorescence spectrophotometer
How do fluorescence spectrophotometers avoid interference?
How do fluorescence spectrophotometers avoid interference?
What does size exclusion chromatography use to separate molecules?
What does size exclusion chromatography use to separate molecules?
How does size exclusion chromatography separate molecules?
How does size exclusion chromatography separate molecules?
What is the primary principle behind dialysis?
What is the primary principle behind dialysis?
How does electrophoresis separate molecules?
How does electrophoresis separate molecules?
What is the main purpose of UV/visible Spectroscopy?
What is the main purpose of UV/visible Spectroscopy?
What happens when a compound absorbs UV energy?
What happens when a compound absorbs UV energy?
How is transmittance calculated in UV spectroscopy?
How is transmittance calculated in UV spectroscopy?
What does high absorbance indicate in UV spectroscopy?
What does high absorbance indicate in UV spectroscopy?
Which law states that light absorption is proportional to the path length?
Which law states that light absorption is proportional to the path length?
At which wavelength does DNA absorb UV light?
At which wavelength does DNA absorb UV light?
Which amino acid side chains absorb UV light around $280/274nm$?
Which amino acid side chains absorb UV light around $280/274nm$?
Which prosthetic group absorbs UV light at $400nm$?
Which prosthetic group absorbs UV light at $400nm$?
Fluorescence spectroscopy uses light to excite electrons, causing them to emit higher energy light.
Fluorescence spectroscopy uses light to excite electrons, causing them to emit higher energy light.
Stoke shift is the term for the difference between excitation and emission wavelengths in fluorescence spectroscopy.
Stoke shift is the term for the difference between excitation and emission wavelengths in fluorescence spectroscopy.
Fluorescence spectrophotometers measure emission at right angles to avoid interference.
Fluorescence spectrophotometers measure emission at right angles to avoid interference.
Dialysis separates molecules based on charge in an electric field.
Dialysis separates molecules based on charge in an electric field.
Agarose gels are used in size exclusion chromatography to separate molecules based on size.
Agarose gels are used in size exclusion chromatography to separate molecules based on size.
Proteins can be separated using electrophoresis, with DNA running in a thinner gel.
Proteins can be separated using electrophoresis, with DNA running in a thinner gel.
SDS-PAGE separates proteins by denaturing them and running them in a thicker gel.
SDS-PAGE separates proteins by denaturing them and running them in a thicker gel.
Size exclusion chromatography separates molecules based on their charge.
Size exclusion chromatography separates molecules based on their charge.
UV energy is similar to the bonding in organic molecules.
UV energy is similar to the bonding in organic molecules.
Absorbance is calculated as log10(I0/I)
Absorbance is calculated as log10(I0/I)
Beer's law states that light absorption is proportional to the number of absorbing molecules (concentration)
Beer's law states that light absorption is proportional to the number of absorbing molecules (concentration)
Lambert's law states that light absorption is proportional to path length (width of sample the light is passed through)
Lambert's law states that light absorption is proportional to path length (width of sample the light is passed through)
DNA absorbs UV light at 260nm.
DNA absorbs UV light at 260nm.
Peptide bond in proteins absorbs UV light at 190nm.
Peptide bond in proteins absorbs UV light at 190nm.
Tryptophan and tyrosine amino acid side chains absorb around 280/274nm.
Tryptophan and tyrosine amino acid side chains absorb around 280/274nm.
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Study Notes
-
Fluorescence spectroscopy involves exciting electrons in a sample with light, causing them to emit lower energy light
-
GFP, a naturally fluorescent protein, is widely used in biotechnology
-
Fluorescent molecules have highly conjugated systems, many rings, and are rigid and planar
-
Stoke shift is the difference between excitation and emission wavelengths, with larger shifts increasing sensitivity
-
Fluorescence spectrophotometers use a light source, prism, slits, and measure emission at right angles to avoid interference
-
Fluorescence offers enhanced sensitivity and specificity, but can be affected by energy transfer and not all compounds are fluorescent
-
Molecules can be separated using techniques like size exclusion chromatography, which uses a column and a mobile and stationary phase
-
Size exclusion chromatography separates molecules based on size, with small molecules entering beads and large ones excluded
-
Dialysis uses a semi-permeable membrane to separate molecules based on size, with small molecules passing through and large ones remaining in solution
-
Electrophoresis separates molecules based on charge in an electric field, with agarose gels acting as a molecular sieve
-
DNA and proteins can be separated using electrophoresis, with DNA negatively charged and separated using agarose gels in a tank.
-
Proteins can be separated using SDS-PAGE, which denatures them and runs them in a thinner gel.
-
Fluorescence spectroscopy involves exciting electrons in a sample with light, causing them to emit lower energy light
-
GFP, a naturally fluorescent protein, is widely used in biotechnology
-
Fluorescent molecules have highly conjugated systems, many rings, and are rigid and planar
-
Stoke shift is the difference between excitation and emission wavelengths, with larger shifts increasing sensitivity
-
Fluorescence spectrophotometers use a light source, prism, slits, and measure emission at right angles to avoid interference
-
Fluorescence offers enhanced sensitivity and specificity, but can be affected by energy transfer and not all compounds are fluorescent
-
Molecules can be separated using techniques like size exclusion chromatography, which uses a column and a mobile and stationary phase
-
Size exclusion chromatography separates molecules based on size, with small molecules entering beads and large ones excluded
-
Dialysis uses a semi-permeable membrane to separate molecules based on size, with small molecules passing through and large ones remaining in solution
-
Electrophoresis separates molecules based on charge in an electric field, with agarose gels acting as a molecular sieve
-
DNA and proteins can be separated using electrophoresis, with DNA negatively charged and separated using agarose gels in a tank.
-
Proteins can be separated using SDS-PAGE, which denatures them and runs them in a thinner gel.
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