BIOCHEMISTRY C785 OA study guide Questions & Answers Latest 2021/2022
1) What is the basic structure of an amino acid? List the 4 groups and describe what they
look like.
+ alpha carbon ©, Amino group ( NH2 or NH3, Carbonyl group( cooh) and variance or
side chain(R group)
2) How do you identify the 3 different types of side chains: non-polar/hydrophobic, polar, and
charged?
Non Polar:::: ( Hydrophobic)- water hating -Ch3 or C and H ( side) special case:
Tryptophan is a hydrophobic nonpolar even tho is has a single N
Polar:::: ( Hydrophilic): OH, NH, ( center). Just O! SH is a special polar called Cysteine
ending in SH.
Charged:::: + or – ( Ionic bond) can be polar.
3) What kind of bonds do each of the 3 different types of side chains make?
answered above: The reason we care about what class an amino acid belongs: So, we know what kind
of interactions it can form to stabilized a protein tertiary structure.
Hydrophobic interact with hydrophobic- C H.
Polar interact via Hydrogen bonds.
+ or – charge interact va Ionic bond
-s-s Cysteine side chain can interact via Disulfide bond.
4) Protein Folding: What are the 4 levels of protein structure? List distinguishing features of each.
- Primary- Linked by peptide bond.
-Secondary-The alpha helix(coil) or pleated sheets.
-Tertiary -Protein folding (3 dimensional shape that is necessary for protein to function.
-quaternary: 2 or more folded amino acid chains come together to make final working protein.
ALL PROTEIN HAVE PRIMARY, SECONDARY AND TERTRIARY BUT SOME ONLY HAVE QUATERNARY
STRUCTURE.
Ex. Myoglobin only has the first 3. Hemoglobin has 4 subunits . Myoglobin only 1 subunits.
-
5) What bonds make up each level of protein structure and how are they formed?
Primary: Peptide bond. Formed by dehydration syntheses. Broken by Hydrolysis ( H20ADD)
Secondary: Hydrogen BOND. Alpha Helix between above and below. Beta sheets Faraway.
Tertiary: hydrophobic interactions: -Weakest but greatest in #!
Hydrogen bond: Stronger than hydrophobic.
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, Ionic bond: Stronger than hydrogen.
Disulfide bond: strongest but fewest in number.
Quaternary: SAME as ABOVE.
6) What environmental change breaks each type of bond?
Disulfide Bond: Strong reducing agent.
Ionic and hydrogen bond: Ph change and high salt concentration.
Hydrophobic: HEAT
Primary – Peptide bonds (backbone)
Secondary – Hydrogen bonds
(backbone)
Tertiary – Hydrophobic interactions,
hydrogen bonds, ionic bonds, disulfide
bonds (side chain)
Quaternary – More than one subunit
held by hydrophobic interactions,
hydrogen bonds, ionic bonds, disulfide
bonds (side chain)
7) What type of amino acid side chain leads to protein aggregation?
-Protein that can denature can aggregate. Its BECUZ of HYDROPHOBIC interaction.
8) How do environmental changes affect protein folding?
Above: - hydrophobic-Heat. H and I: PH and Salt. Dis: reducing agent.
9) How do mutations affect protein structure?
-
10) How do enzymes catalyze reactions? By Lowering activation energy and increasing RATE.
This study source was downloaded by 100000830214522 from CourseHero.com on 04-09-2022 06:09:17 GMT -05:00
https://www.coursehero.com/file/67421503/OA-study-guidedocx/
1) What is the basic structure of an amino acid? List the 4 groups and describe what they
look like.
+ alpha carbon ©, Amino group ( NH2 or NH3, Carbonyl group( cooh) and variance or
side chain(R group)
2) How do you identify the 3 different types of side chains: non-polar/hydrophobic, polar, and
charged?
Non Polar:::: ( Hydrophobic)- water hating -Ch3 or C and H ( side) special case:
Tryptophan is a hydrophobic nonpolar even tho is has a single N
Polar:::: ( Hydrophilic): OH, NH, ( center). Just O! SH is a special polar called Cysteine
ending in SH.
Charged:::: + or – ( Ionic bond) can be polar.
3) What kind of bonds do each of the 3 different types of side chains make?
answered above: The reason we care about what class an amino acid belongs: So, we know what kind
of interactions it can form to stabilized a protein tertiary structure.
Hydrophobic interact with hydrophobic- C H.
Polar interact via Hydrogen bonds.
+ or – charge interact va Ionic bond
-s-s Cysteine side chain can interact via Disulfide bond.
4) Protein Folding: What are the 4 levels of protein structure? List distinguishing features of each.
- Primary- Linked by peptide bond.
-Secondary-The alpha helix(coil) or pleated sheets.
-Tertiary -Protein folding (3 dimensional shape that is necessary for protein to function.
-quaternary: 2 or more folded amino acid chains come together to make final working protein.
ALL PROTEIN HAVE PRIMARY, SECONDARY AND TERTRIARY BUT SOME ONLY HAVE QUATERNARY
STRUCTURE.
Ex. Myoglobin only has the first 3. Hemoglobin has 4 subunits . Myoglobin only 1 subunits.
-
5) What bonds make up each level of protein structure and how are they formed?
Primary: Peptide bond. Formed by dehydration syntheses. Broken by Hydrolysis ( H20ADD)
Secondary: Hydrogen BOND. Alpha Helix between above and below. Beta sheets Faraway.
Tertiary: hydrophobic interactions: -Weakest but greatest in #!
Hydrogen bond: Stronger than hydrophobic.
This study source was downloaded by 100000830214522 from CourseHero.com on 04-09-2022 06:09:17 GMT -05:00
https://www.coursehero.com/file/67421503/OA-study-guidedocx/
, Ionic bond: Stronger than hydrogen.
Disulfide bond: strongest but fewest in number.
Quaternary: SAME as ABOVE.
6) What environmental change breaks each type of bond?
Disulfide Bond: Strong reducing agent.
Ionic and hydrogen bond: Ph change and high salt concentration.
Hydrophobic: HEAT
Primary – Peptide bonds (backbone)
Secondary – Hydrogen bonds
(backbone)
Tertiary – Hydrophobic interactions,
hydrogen bonds, ionic bonds, disulfide
bonds (side chain)
Quaternary – More than one subunit
held by hydrophobic interactions,
hydrogen bonds, ionic bonds, disulfide
bonds (side chain)
7) What type of amino acid side chain leads to protein aggregation?
-Protein that can denature can aggregate. Its BECUZ of HYDROPHOBIC interaction.
8) How do environmental changes affect protein folding?
Above: - hydrophobic-Heat. H and I: PH and Salt. Dis: reducing agent.
9) How do mutations affect protein structure?
-
10) How do enzymes catalyze reactions? By Lowering activation energy and increasing RATE.
This study source was downloaded by 100000830214522 from CourseHero.com on 04-09-2022 06:09:17 GMT -05:00
https://www.coursehero.com/file/67421503/OA-study-guidedocx/
