Chapter 18: Problem 24
How does glucose differ structurally from sucrose?
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Key Concepts
These are the key concepts you need to understand to accurately answer the question.
Chapter 18: Problem 24
How does glucose differ structurally from sucrose?
These are the key concepts you need to understand to accurately answer the question.
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Get started for freeHow does the sequence of amino acids influence a protein. Can swapping just two amino acids in a very large protein molecule affect its function? Explain by giving an example.
How many different tripeptides can be made that contain the amino acids alanine, serine, and glycine?
Amino acids are a sort of self-contradiction because they contain both a basic group (the \(\mathrm{NH}_{2}\) end) and an acidic group (the \(\mathrm{CO}_{2} \mathrm{H}\) end \()\) in the same molecule. Therefore, it should not surprise you that, when dissolved in water, an amino acid can react with itself to form what is known as a zwitterion. Based on this information, (a) Draw the structural formula for the form of the amino acid alanine you would expect to find in a neutral water solution. What is the net electrical charge on this species? (b) Enough concentrated \(\mathrm{HCl}\) is added to the solution of part (a) to make it strongly acidic. Draw the structural formula for the form of alanine you expect to find in this solution. What is the net charge on the alanine? (c) Enough concentrated \(\mathrm{NaOH}\) is added to the solution of part (a) to make it strongly basic. Draw the structural formula for the form of alanine you expect to find in this solution. What is the net charge on the alanine now?
What is a polymer? How does it differ from a monomer?
In an amino acid, a carbon atom bound directly to the carbonyl carbon of the acid function is called the alpha carbon \((\alpha\) -carbon \() .\) Draw glycine, point out the \(\alpha\) -carbon, and then explain why all 20 amino acids used to build human proteins are called \(\alpha\) -amino acids. Then draw the simplest \(\beta\) -amino acid.
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