GOB Chemistry
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True or False: α-keratin and tropocollagen have the same secondary and tertiary structure and only mainly differ in their amino acid composition.
Amino acid side chain interactions primarily influence the overall shape of proteins. Among the following pairs of amino acids, identify which participate in hydrophobic interactions.
i. Ser · · ·Thr
ii. Leu · · · Ala
iii. Val · · · Ile
iv. Lys · · · Glu
Identify the type of molecular interactions or bonds formed between the side chains of the amino acids methionine and valine.
Determine the type of bond formed between the side chains of lysine and aspartic acid.
For each of the following pairs of amino acids, indicate whether the bond formed between their side chains is covalent or noncovalent.
i. Lysine and glutamine
ii. Asparagine and threonine
iii. Cysteine and cysteine
iv. Valine and phenylalanine
Which of the following is primarily responsible for the influence of glutamine on the tertiary structures of proteins?
Octreotide is a growth hormone inhibitor, and it is used to treat disorders caused by excess growth hormone. It is a polypeptide with a primary structure of Phe-Cys-Phe-Trp-Lys-Thr-Cys-Thr. Its structure has a cyclic configuration held by a disulfide bridge. Using their abbreviations, the structure of octreotide and show the disulfide bridge.
Identify the noncovalent interaction that results in proteins folding into a globe-like shape, forming a 'water-loving' exterior. Give two examples of amino acids that will have this interaction.
In a tertiary protein structure, which type of interaction occurs between the following R groups?
Below are R groups of two amino acids. (i) Identify these two amino acids and (ii) their type of interaction in tertiary protein structure.
What specific kind of interaction can be expected between alanine and valine within the internal structure of a folded protein?
If all serine is replaced with leucine in a protein, what would you expect from the protein's tertiary structure?
Identify which amino acid below has an R group that would form salt bridges.
Identify the type of interaction between the side chains of threonine and glutamine in a tertiary structure.
In a membrane protein consisting of 180 amino acids, half of them have nonpolar R groups. Given the protein's role in a hydrophobic lipid bilayer, where would these nonpolar amino acids most likely be located in the protein's tertiary structure?
A globular enzyme is found to contain 250 amino acids, with roughly 60% having a polar R group. Considering its aqueous cellular environment, where would these polar amino acids most likely be situated within the enzyme's tertiary structure?