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(1) Describe what you see, using terms that indicate the type of secondary structure shown. (2) What can you conclude about p

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Answer #1

1. There are two types of secondary structure alpha helix and beta sheet. In alpha helix first amino acid make bond with fifth amino acid that is if first amino acid is n then it will make bond with n+4 amino acid. Alpha helix show colied structure.

2. Since in this protein amino acids which is exposed is leucine given in question which is a non polar amino acid which do not interact with water and this is present in inside so there must be hydrophobic environment and thus outer environment will be hydrophilic. Thus cellular location of this protein is cytoplasm.

3. Leucine is hydrophobic amino acid it can't be present in hydrophilic environment so itbis present inside the core.

4. The number indicate the position of that particular amino acid and letter indicate the name of that amino acid. This is a homodimer since it appears like both the alpha helices are exactly same and have leucine at same position in both the polypeptides.

6.The residues involved in the H bonding are seperated by 3 residues. Since in alpha helix n amino acid make hydrogen bond with n+5th amino acid , so in between 3 amino acid comes. There is a difference in bonds, the amino acid make backbone or peptide chain by peptide bond and side chain interact with other side chain with hydrogen bonding.

(Due to time bound and HOMEWORKLIB RULES I am only able to solve 4 questions however I also solved one more question but due to time bound I am not able to solve next two questions, so can you please post the nest two questions again or specify to slove snly that two questions. And if you like these answers please upvote for it)

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