Question

Create a sequence of a 21-amino acid peptide that you think would self-assemble into a coiled-...

Create a sequence of a 21-amino acid peptide that you think would self-assemble into a coiled- coil structure. Design one. Underline the hydrophobic and polar amino acids in the sequence.

Homework Answers

Answer #1

The sequence could be

Alanine-Cysteine-Glutamine-Threonine-Phenylalanine -Tyrosine-Tryptophan-Isoleucine-Glutamine -Serine -Aspargine-histidine-tyrosine-proline-methionine-histidine-tryptophan-glycine-cysteine-Asparagine-glutamine

the squence could be as mentioned above

The hydrophobic amino acids are marked bold and underligned

the other are polar amino acid.

The peptide is formed due to amid linkage between amino acids, they undergo coiling due to hydrogen bonds.

Know the answer?
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for?
Ask your own homework help question
Similar Questions
Draw a peptide chain that includes up to 7 amino acids. Show their sequence by drawing...
Draw a peptide chain that includes up to 7 amino acids. Show their sequence by drawing the structure of each amino acid present in their chain, & calculate the net ionic charge on that peptide at a certain pH (any pH).
Assuming 1. Amino acid 212 is changed from Glycine to Alanine in warm adapted species. Amino...
Assuming 1. Amino acid 212 is changed from Glycine to Alanine in warm adapted species. Amino acid 216 is changed from Glutamine to Lysine in warm adapted species. Amino acid 219 is changed from Theornine to Alanine in warm adapted species. Amino acid 220 is changed from Asparatie to Glutamate warm adapted species. 2. Both Glycine and Alanine are non polar amino acids. Glutamine is uncharged while lysine is positively charged Threonine is polar uncharged while Alanine is hydrophobic Both...
The following peptide fragments were generated after digestion of an 11 amino acid polypeptide with trypsin...
The following peptide fragments were generated after digestion of an 11 amino acid polypeptide with trypsin and separately with thermolysin: Trypsin: PA, YI, YKA, FDRH Thermolysin: HYI, PAYK, AFDR What is the sequence of the parent polypeptide? Please show how you arrived at your answer! (Note that trypsin recognizes the basic amino acids lysine (K) and arginine (R) and cleaves the peptide bond just after those; thermolysin recognizes the aromatic amino acids tyrosine (Y), phenylalanine (F), tryptophan (W), along with...
Biochemists who study protein structure and function often introduce mutations (changes) to a protein's amino acid...
Biochemists who study protein structure and function often introduce mutations (changes) to a protein's amino acid sequence. One common change is an amino acid substitution that can creates a modified protein that can mimic (function similar to) a phosphorylated protein. Using what you know about different amino acids, which amino acid(s) would be a good choice for this change to a phosphorylated-like state? Briefly explain why.
Which type of qualifier would most likely contain the amino acid sequence of a protein as...
Which type of qualifier would most likely contain the amino acid sequence of a protein as one of its attributes in a GenBank record? 1. gene 2. source 3. mRNA 4. CDS
1.     The primary sequence of the peptide listed below. H2N - Asp-Thr-Phe-Lys-COOH H2N – D -T...
1.     The primary sequence of the peptide listed below. H2N - Asp-Thr-Phe-Lys-COOH H2N – D -T – F – K – COOH Use the one letter amino acid code and identify from N-terminus to C-terminus. a.     Determine the pI of the peptide. (Round to 2 decimal points) b.     Would mutating residue #3 to Ala change the pI of the peptide? Explain. c.      Which type of noncovalent interaction would the indicated residue side chain make at the given pH? (H-bond, Hydrophobic...
What would happen to a protein like signal peptidase if you removed its signal peptide but...
What would happen to a protein like signal peptidase if you removed its signal peptide but added a nuclear localization signal (NLS)? It would end up in the nucleus. It would end up in the cytoplasm It would be secreted None of the above What would happen to a secreted protein (e.g. insulin) if you produced it from an mRNA missing the sequence encoding the signal peptide? It would be properly secreted, though it might not fold correctly. It would...
Are there any amino acids that you think would make a good buffer at pH=8.0? Why?...
Are there any amino acids that you think would make a good buffer at pH=8.0? Why? List them.
Which statements are TRUE of both α helices and β sheets? Multiple answers: You can select...
Which statements are TRUE of both α helices and β sheets? Multiple answers: You can select more than one option A Found in the same percentage in all proteins B Stabilized by H bonds between –NH and –CO groups C Found in globular proteins D Affected by amino acid sequence E An extended conformation of the polypeptide chain F Includes all 20 standard amino acids in equal frequencies G Hydrophobic interactions are responsible for the primary structure
Degenerate codons as you mentioned can code the same amino acid. You claimed it as one...
Degenerate codons as you mentioned can code the same amino acid. You claimed it as one gene coding for different polypeptides. Would the nucleotide sequence change still be accounted as a single gene?
ADVERTISEMENT
Need Online Homework Help?

Get Answers For Free
Most questions answered within 1 hours.

Ask a Question
ADVERTISEMENT