Question

d. BC e. a and b f. None of the above 14) Briefly, describe whether you would expect the change in Trp fluorescence intensity to be greater for a protein-protein binding interaction or for protein folding/unfolding and justify your answer. 2 pts 15 Briefly, describe why CD spectroscopy would be a superior technique for analyzing the structure of the following protein sequence compared to UV Nis spectroscopy. 2 pts SEQUENCE: LAVISREPPIHGGSQCMNNHIPPKLFF

Answer 1

14

Fluorosence spectroscopy is spectroscopy that analyse fluorosence of sample

Trp fluorosence ( tryptophan) is fluorosence of folded protein that is from individual aromatic residues

It differs due to hydrophobic core part and also due to surfactant addition red and blue shift respectively

Electrostatic interactions are imp in protein

Ans. Protein binding normally lead to addition of 3D structure or its change which gives more intensity of maximum wavelength

Protein folding and unfolding also lead change in intensity but not as binding

As here the curve of folded to unfolded intensity decreases but peak move to shorter maximum wavelength

15

CD circular dichroism electroscopy uses optically active substance

And determine by left and right chiral movement

This spectroscopy lead to even know the bond and organic compound structre and verify sequence also

But uv vis is used to determine secondary structure of protein

First one is more specific

So it can be used for this study