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First blank: A phosphate/a carboxyl/a sulfhydryl/a carbonyl 2nd is the image (di

ID: 183531 • Letter: F

Question

First blank: A phosphate/a carboxyl/a sulfhydryl/a carbonyl 2nd is the image (direction is there) 3rd: yes or no 4th blank: tertiary/ secondary/ quaternary/ primary
5. How protein primary structure affects protein folding and shape The following diagram represents a properly folded protein molecule dissolved peptide backbone of the protein, while the five grey boxes represent the R groups of five amino acids located in various positions along this protein: two cysteines, one glutamine, one in water. The black line represents the isoleucine, and one serine. The red cross within the rightmost grey box indicates the position of the serine along this protein. This particular serine is special because it has been modified with group. Predict where the remaining four a mino acids belong in the protein, based on their functional groups and affinity for water molecules, which surround the outside of the protein. Drag each of their corresponding points into the correct grey box. Cysteine 12 Glutamine [1) OH lsoleucine (1) HS HoOC rom what you can see, have any disulfide linkages formed within this protein?[ -] he structure of a protein is defined by its amino acid sequence. Ignoring the unidentified amino ids in the sequence, which of the following is the correct order for the amino acids you identified? N-terminal end-cysteine-Isoleucine-cysteine-Glutamine-C-terminal end O N-terminal end-Isoleucine-Cysteine-Cysteine-Glutamine-C-terminal end O N-terminal end-Isoleucine-Cysteine-Cysteine-Isoleucine-C-terminal end O N-terminal end-Glutamine-Cysteine-Cysteine-Isoleucine-C-terminal end

Explanation / Answer

1) A carboxyl group

2) SH----- cystenine

HS--------cystenine

H3N---------glutamine

hooc- isoleucine

3)No

A disulfide bond, also known as an S-S bond, or disulfide bridge, is a covalent bond derived from two thiol groups.

4)Primary

The primary shape of a protein — its amino acid sequence — drives the folding and intramolecular bonding of the linear amino acid chain, which in the long run determines the protein's particular three-dimensional form