Concept explainers
Interpretation:
Example of a protein containing primarily alpha-helices and also identify the protein mentioned is globular or fibrous.
Concept introduction:
Many amino acids are linked together through amide bonds to form a biologically large molecule known to be proteins.
Amino
Secondary structure of protein is the repeating structural patterns (
Fibrous protein is a tough, water insoluble protein whose protein chains form fibers or sheets.
Globular protein is a water soluble protein whose chain is folded in a compact shape.
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Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
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- Many transmembrane proteins have a large series of hydrophobic amino acids such as those in the middle of the protein (around b). Why would this make sense, and where would you expect these to be located in the final protein structure?arrow_forwardIn the figure below, protein 1 is located in the cytosol, and protein 2 is membrane bound. Give 3 specific examples from Figure 4-3 of amino acids that you might expect to find on the surface of protein 1. For protein 2, give three specific amino acids that you would expect to be on the surface near both points A and B (labeled with stars). To clarify, you should choose 3 amino acids for point A and also list three amino acids for point B. All of the amino acids you choose for Protein 2 must be different from those that you choose for Protein 1. Rationalize your choices by discussing the amino acids you chose, and their properties in a few sentences. Protein 1 Protein 2arrow_forwardConsider protein folding that results when the following components interact: Where the solution is at a pH of 7, green (thick-dotted line) represents aspartic acid (R group contains a carboxylic acid with pKa = 4), orange (thick-solid line) represents lysine (R group contains an amine with pKa = 10), and blue (thin-solid line) represents hydrophilic groups. Rank the three complexes in order from lowest to highest dissociation constants Kd (low Kd values correspond to good binding constants and low energy, while high Kd values correspond to low binding constants and high energy) as determined by intermolecular charge-charge interactions. For those complexes with charge-charge interactions being equal, look at the possibility for the formation of hydrogen bonds via carboxylic acid dimers (only possible when the carboxylic acid is protonated) which are low energy structures.arrow_forward
- Disulfide linkages are uncommon in cytoplasmic proteins, whereas they are common in extracellular proteins. Why?arrow_forwardHOW MANY DIFFERENT PROTEINS CAN BE CONSTRUCTED THAT ARE EXACTLY FOUR AMINO ACIDS LONG? (HINT: THERE ARE 20 POSSIBLE AMINO ACIDS.)arrow_forwardConsider beta-sheet comprised of twelve amino acid residues (two strands of six residues each). How many hydrogen bonds should be formed between backbone atoms in this sheet?arrow_forward
- When a protein was denatured and lost its function due to its spatial structures were disrupted. Which of the following was disrupted during the denaturing process?arrow_forwardWhich fibrous protein is found in connective tissue and consists of 3 left-handed helices twisted together?arrow_forwardDescribe the general structure of a type 2 alpha helix protein. Explain how type 2 alpha helix transmembrane domains can be used to form pathways for large polar and charged molecules to traverse the lipid bilayer of the cell membrane.arrow_forward
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