You are supplied with an unknown protein that consists of more than 130 amino acids. Furthermore this protein consists of just 1 polypeptide chain. Explain (in detail) how you would determine the primary structure of this protein
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- Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.Hemoglobin is a tetramer consisting of two α and two β chains.What level of protein structure is described in this statement?Hemoglobin is a tetramer consisting of two a and two b chains. What level of protein structure is described in the above statement?
- You are supplied with an unknown protein that consists of more than 130 amino acids. Furthermore this protein consists of just 1 polypeptide chain. Explain how you would determine the primary structure of this protein.the sequence of amino acids in a protein is known as the secondary structure true or false?For the protein given in the attached picture: Write the name of these 5 amino acids corresponding to their abbreviation of 3 letters. Describe precisely how the functional groups in the amino acids are involved in bonding between two successive amino acids in the protein.
- Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid stronger in the hydrophobic interior of a protein than in aqueous solvent (water)?When two simple proteins, A and B, are separately hydrolysed and subjected to amino acid analysis, they yield exactly the same results in terms of the number and type of amino acids. Can you confidently conclude that the two proteins have the same primary structure? Justify your answer.Why do small proteins have more difficulty folding and holding shape than larger proteins? If you were designing a small protein, what elements of structure might you include to increase protein stability?
- Name another condition besides heat and exposure to a bond disruptor (like alcohol) that could affect the ability of a protein to maintain its shape.At what level of protein structure (primary, secondary, tertiary or quarternary) does Hydrogen bonding is relevant ? Consider if there is no Hydrogen bonding that exists, and only van der Waals exists in this protein structure, what do you expect to happen in its property? Explain with examples.In the illustration below, the blue squiggly line represents a protein. Notice that the amino acid that is colored red and the amino acid that is colored black are very close to each other in space, but they are far from each other in the primary structure of this protein. How can you explain why two amino acids that are so far from each other in the primary structure of a protein can be so close together in the tertiary structure of the same protein?
