Feb 14, 24th, 26th, 28th

Question 1

•Amino acids contain
_________________
groups, bonded to a _____ carbon (α) with a hydrogen and a R group.
•_ ______(side chain) is variable and determines unique character of amino acid.
•Two amino acids are joined together by a ____________________
carboxyl group and amino group by a _________ reaction.
between the
•Polypeptides are linear chains of ______ ___ linked by ________ bonds.
•Proteins are ______ and (may) contain multiple __________.
3

Answer 1

•Amino acids contain
_amino and a carboxyl
groups, bonded to a central carbon (α) with a hydrogen and a R group.
•R group (side chain) is variable and determines unique character of amino acid.
•Two amino acids are joined together by a __covalent peptide bond between
carboxyl group and amino group by a dehydration reaction.
•Polypeptides are linear chains of amino acids linked by peptide bonds.
•Proteins are folded and (may) contain multiple polypeptides.
3

Question 2

______________________________
• R groups usually contain –CH2 or –CH3
______________________________
• R groups usually contain oxygen (or -OH)
______________________________
• R groups that contain acids or bases that can ionize
________ amino acids:
• R groups contain a carbon ring with alternating single and _____ bonds
________ functional amino acids include:
1. ______________________: first amino acid in polypeptide
2. ______________________: causes bend in polypeptide chains
3. ______________________: disulfide bridge contributes to structure of
polypeptides
Do know the information on the right.
Do NOT need to memorize the structures of the R
groups, nor which amino acids are in which categories. 4

Answer 2

____Nonpolar amino acids
• R groups usually contain –CH2 or –CH3
____uncharged polar amino acids
• R groups usually contain oxygen (or -OH)
__charged amino acids
• R groups that contain acids or bases that can ionize
Aromatic amino acids:
• R groups contain a carbon ring with alternating single and double bonds
Special functional amino acids include:
1. methionine : first amino acid in polypeptide
2. ___proline_____: causes bend in polypeptide chains
3. ____cysteine : disulfide bridge contributes to structure of
polypeptides
Do know the information on the right.
Do NOT need to memorize the structures of the R
groups, nor which amino acids are in which categories. 4

Question 3

•1° (primary) _______________________ (ultimately)
determines protein folding and 3-D structure which is critical for
proper function. (But the primary structure is simply the amino acid sequence)
•2° (secondary) structure depends on hydrogen bonding in the polypeptide
backbone (α-helices and β-sheets).
•3° (tertiary) structure is the 3-D structure of a single polypeptide and is
composed of interactions between amino acid side chains.
• 4° (quaternary) structure are interactions between more than one polypeptide
to form a multisubunit protein (e.g. hemoglobin)
•When protein folding is disrupted by heat, chemicals, or mutations that change
the amino acid sequence, this is called _____________________
.
•
_____________________ function to protect slow-folding or denatured proteins
by preventing their aggregation
•Diseases associated with misfolded proteins: Alzheimer’s, Parkinson’s and
Creutzfeldt-Jakob

Answer 3

•1° (primary) ___amino acid sequence (ultimately)
determines protein folding and 3-D structure which is critical for
proper function. (But the primary structure is simply the amino acid sequence)
•2° (secondary) structure depends on hydrogen bonding in the polypeptide
backbone (α-helices and β-sheets).
•3° (tertiary) structure is the 3-D structure of a single polypeptide and is
composed of interactions between amino acid side chains.
• 4° (quaternary) structure are interactions between more than one polypeptide
to form a multisubunit protein (e.g. hemoglobin)
•When protein folding is disrupted by heat, chemicals, or mutations that change
the amino acid sequence, this is called ___denaturation
.
•
___chaperones _ function to protect slow-folding or denatured proteins
by preventing their aggregation
•Diseases associated with misfolded proteins: Alzheimer’s, Parkinson’s and
Creutzfeldt-Jakob