Predict the effects of changing Phe 34, Ser 36, and Trp 108 to Lys on hen egg white lysozyme catalysis, assuming that this change does not significantly alter the 3-D structure of the protein.

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Collen VonLv2

11 Apr 2019

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4. It is possible to make some predictions about protein secondary structure based on the primary sequence. Consider the following amino acid sequence.

Ile-Ala-His-Thr-Tyr-Gly-Pro-Phe-Glu-Ala-Ala-Met-Cys-Lys-Trp-Glu-Ala-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe-His-Arg

(a) Where might B turns occur?

(b) Where might intrachain disulfide cross-linkages be formed?

(c) Assuming that this sequence is part of a larger globular protein, what is the probable location (exterior or interior of the protein) of the amino acid residues and explain your reasoning.

Asp Ile Thr Ala Gln Lys

tauperaven764

For the following strand of DNA, use the table below to provide: bases for the complementary mRNA and the associated amino acids. What do you notice about the genetic code for proline in the peptide? How would the loss of the first G or switching that G to a T affect the structure and function of this protein?

DNA: GGC CTA CAA GCC GGA ACA GTT ACC GCG TAA CGA

RNA: ??? ??? ??? ??? ??? ??? ??? ??? ??? ??? ???

Amino Acid:??? ??? ??? ??? ??? ??? ??? ??? ??? ??? ???
(3 Letters)

Genetic Code Table (mRNA)

1st position (5' end)	2nd position (middle)				3rd position (3' end)
1st position (5' end)	U	C	A	G	3rd position (3' end)
U	Phe F Phe F Leu L Leu L	Ser S Ser S Ser S Ser S	Tyr Y Tyr Y STOP STOP	Cys C Cys C STOP Trp W	U C A G
C	Leu L Leu L Leu L Leu L	Pro P Pro P Pro P Pro P	His H His H Gln Q Gln Q	Arg R Arg R Arg R Arg R	U C A G
A	Ile I Ile I Ile I Met M	Thr T Thr T Thr T Thr T	Asn N Asn N Lys K Lys K	Ser S Ser S Arg R Arg R	U C A G
G	Val V Val V Val V Val V	Ala A Ala A Ala A Ala A	Asp D Asp D Glu E Glu E	Gly G Gly G Gly G Gly G	U C A G

turquoisewater-buffalo47

Answer the following questions concerning the polypeptides whose amino acid sequences are shown below. Explain your reasoning for all.

A) Gly-Ile-Trp-Leu-Ile-Ile-Phe-Gly-Val-Val-Ala-Gly-Val-Ile-Gly-Trp-Ile-Leu-Leu-Leu

B) Gly-Pro-Asp-Gly-Pro-Met-Gly-Pro-Ser-Gly-Pro-Arg-Gly-Pro-Glu-Gly-Pro-Asp-Gly

C) Gly-Met-Trp-Pro-Glu-Met-Cys-Gly-Glu-Pro-Ala-His-Val-Arg-Asp-Tyr-Pro-Leu-Leu

D) Gly-Met-Trp-Pro-Glu-Met-Cys-Gly-Glu-Pro-Ala-His-Val-Arg-Asp-Tyr-Cys-Leu-Leu

1. Which would be most likely to form an a-helical structure?

2. Which could have at least one disulfide bond?

3. Suppose that the first amino acid residue in peptide (1) were altered from Gly to Pro. Would you expect this change to have an effect on the secondary structure of this peptide? Why or why not?