Biochemistry: Tryptophan fluorescence

Your summary is almost done!In summary, a 100-residue globular protein with two Trp residues and two segments with the sequence SSSLWLAAA (residues 1-9 and 44-53) is being discussed in terms of its fluorescence spectrum. Based on information from a biochem lecture, it is known that when Trp is buried in the protein, it has a wavelength of 320 nm, while when it is on the outside, it has a wavelength of 350 nm. Therefore, the most likely answer to the question about the protein's fluorescence spectrum is c) - a single band at 320 nm.
  • #1
Jef123
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1. A 100-residue globular protein contains two Trp residues, and has two segments with the same 9-amino acid sequence, SSSLWLAAA. One segment is residues 1-9, and one segment is residues 44-53. What would the complete fluorescence spectrum of the protein MOST LIKELY contain?

a) It would contain a single band at 350 nm
b) Two bands, one at 350 nm, and one at 320 nm
c) It would contain a single band at 320 nm
d) it would contain a single band at 335 nm2. This is all info from my biochem lecture, so I'm not sure what to include other than when Trp is "buried" in the protein it has a wavelength of 320 nm and when it is on the outside of the protein it has a wavelength of 350 nm.

The Attempt at a Solution

: I was thinking that because Trp is surrounded by hydrophobic amino acids it is likely to be buried in the protein, so my answer is c). I don't know the answer to this question though[/B]
 
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  • #2
Thanks for the post! Sorry you aren't generating responses at the moment. Do you have any further information, come to any new conclusions or is it possible to reword the post?
 

1. What is tryptophan fluorescence?

Tryptophan fluorescence is a phenomenon where the amino acid tryptophan emits light when excited by ultraviolet (UV) light. This is due to the presence of a chemical group called an indole ring in tryptophan, which is responsible for its fluorescence.

2. How is tryptophan fluorescence used in biochemistry?

In biochemistry, tryptophan fluorescence is used as a tool to study protein structure and function. Since tryptophan is a relatively rare amino acid, its fluorescence can be used to monitor changes in protein conformation and interactions, as well as enzyme activity.

3. What factors affect the fluorescence of tryptophan?

The fluorescence of tryptophan can be influenced by several factors, including the polarity of its environment, the presence of other nearby amino acids, and changes in pH or temperature. Additionally, the fluorescence intensity can be affected by the orientation of the tryptophan residue within the protein structure.

4. How is tryptophan fluorescence measured?

Tryptophan fluorescence is typically measured using a spectrofluorometer, which detects and measures the emitted light from the tryptophan residue. The fluorescence intensity is recorded as a function of the excitation wavelength, and can provide information about the environment and interactions of the tryptophan residue.

5. What are the applications of tryptophan fluorescence in research?

Tryptophan fluorescence has a wide range of applications in research, including protein structure determination, protein-protein interactions, enzyme kinetics studies, and drug discovery. It is also commonly used in the fields of biochemistry, biophysics, and pharmaceuticals to study the structure and function of proteins and other biomolecules.

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