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Due March 7th: Carbohydrate Practice Questions:
1. Give the empirical formula of a monosaccharide and identify two functional groups that it possesses. (IBHL 1999)
2. Draw the straight chain formula of glucose. Describe the structural difference between an a and a b glucose and name the type of isomerism they exhibit. (IBHL 1999)
3. Write a balanced equation to represent the formationof a disaccharide from glucose/ Explain how this process is extended to the formation of a polysaccharide such as starch. (IBHL 1999)
4. How is the structure different between starch and cellulose?
5. What are the three major functions of polysaccharides in the body?
6. What is glycogen? Describe its structure? Where is it stored in animals?
7. What is the link called that is formed between two monosaccharides to form a disaccharide? What kind of reaction must occur to form this link?
PROTEINS/AMINO ACID PRACTICE (In class – Tues. March 8th)
1. Polypeptides and proteins are formed by the condensation reactions of amino acids.
(a) Give the general structural formula of a 2-amino acid.
(b) Give the structural formula of the dipeptide formed by the reaction of alanine and glycine.
State the other substance formed during this reaction.
(c) State two functions of proteins in the body.
2. The structures of the amino acids cysteine and serine are shown in your table of amino acids They can react with each other to form a dipeptide.
(a) State the type of reaction occurring when amino acids react together and identify the other product of the reaction.
(b) Draw the structures of the two possible dipeptides formed in the reaction between one molecule of each of cysteine and serine.
(c) Six tripeptides can be formed by reacting together one molecule of each of the amino acids arginine, histidine and leucine. Predict the primary structures of these six tripeptides using the three letter symbols shown in on your amino acid table to represent the amino acids.
3. When many amino acid molecules react together a protein is formed. These proteins have primary, secondary and tertiary structures.
(i) State the type of intermolecular force responsible for maintaining the secondary structure.
(ii) State two other ways in which the tertiary structure of the protein is maintained.
4. Explain how paper chromotography and electophoresis can be used to separate amino acids
A. Paper chromotography: Be specific and detailed
B. Electrophoresis: Be very specific and detailed!
5. What is meant by the term peptide linkage. Draw structural formulas to illustrate the formation of a peptide bond
