UNE BIOCHEM UNIT 1 CONTENT EXAM QUESTIONS
AND ANSWERS
The fundamental protein structure is a chain of amino acids (e.g., gly-x-y-gly-x-
y).
There are four primary types of secondary protein structure: ANSWER 1. Alpha
helix.
2. Beta pleated sheets.
3. bends or curves
4. Loops
Which is more stable? Alpha helices or beta sheets?
What maintains these additional structures? - ANSWER beta sheets are more
stable (more hydrogen bonds)
H-bonds stabilize these structures.
___ is produced between carbonyl oxygen bonds and the amide nitrogen of
another peptide four residues ahead. - ANSWER Alpha helices.
What chemical is rarely found in alpha helices, and why? - ANSWER Proline
It kinks the helix
___ are generated when beta-strands are linked laterally by 2-3 hydrogen bonds
(i.e. 2+ peptide chains). - ANSWER Beta sheets
,H-bonds connect the C-O and N-H groups.
Beta sheets can be parallel or antiparallel (answer true).
Short, non-randomized lengths of polypeptide chains that connect two
secondary structures - ANSWER bends, turns, loops
stabilized by: H-bonds, salt bridges, and hydrophobic processes.
Tertiary protein structures are the interactions between secondary structures.
Examples: motifs and domains.
Domains are protein sections that are adequate to complete a task.
motifs: common groupings of secondary structures that form a tertiary
arrangement.
Quarternary protein structures are the interactions of two or more tertiary
subunits to generate a functioning enzyme or unit.
What are the binding proteins for myoglobin and hemoglobin?
And why? - ANSWER Bind oxygen.
homologous proteins (similar basic sequences and functions)
, They bind oxygen because oxygen is insoluble in many fluids (like blood), thus
we require an oxygen transporter.
What are the mechanisms that stabilize tertiary and secondary protein
structures? (3 Things) - Answer: hydrophobic interactions.
Hydrogen bonding.
Salt bonding.
Hemoglobin goes via the blood, heart, and muscle.
Myoglobin goes through (blood, heart, muscle) - ANSWER hemoglobin =
blood (RBCs)
Myoglobin = heart and muscle.
A protein that lacks its ligand or ligands - ANSWER apoprotein
(i.e., haemoglobin without heme)
a protein with its ligand that allows it to function - ANSWER haloprotein.
(i.e. hemoglobin is linked to heme).
What to know about heme - ANSWER 1. iron-containing pyrrole ring in the
center (for O2 binding).
2. it is regarded a prosthetic group (tightly attached to the globin)
Which has a higher oxygen affinity, myoglobin or hemoglobin?
AND ANSWERS
The fundamental protein structure is a chain of amino acids (e.g., gly-x-y-gly-x-
y).
There are four primary types of secondary protein structure: ANSWER 1. Alpha
helix.
2. Beta pleated sheets.
3. bends or curves
4. Loops
Which is more stable? Alpha helices or beta sheets?
What maintains these additional structures? - ANSWER beta sheets are more
stable (more hydrogen bonds)
H-bonds stabilize these structures.
___ is produced between carbonyl oxygen bonds and the amide nitrogen of
another peptide four residues ahead. - ANSWER Alpha helices.
What chemical is rarely found in alpha helices, and why? - ANSWER Proline
It kinks the helix
___ are generated when beta-strands are linked laterally by 2-3 hydrogen bonds
(i.e. 2+ peptide chains). - ANSWER Beta sheets
,H-bonds connect the C-O and N-H groups.
Beta sheets can be parallel or antiparallel (answer true).
Short, non-randomized lengths of polypeptide chains that connect two
secondary structures - ANSWER bends, turns, loops
stabilized by: H-bonds, salt bridges, and hydrophobic processes.
Tertiary protein structures are the interactions between secondary structures.
Examples: motifs and domains.
Domains are protein sections that are adequate to complete a task.
motifs: common groupings of secondary structures that form a tertiary
arrangement.
Quarternary protein structures are the interactions of two or more tertiary
subunits to generate a functioning enzyme or unit.
What are the binding proteins for myoglobin and hemoglobin?
And why? - ANSWER Bind oxygen.
homologous proteins (similar basic sequences and functions)
, They bind oxygen because oxygen is insoluble in many fluids (like blood), thus
we require an oxygen transporter.
What are the mechanisms that stabilize tertiary and secondary protein
structures? (3 Things) - Answer: hydrophobic interactions.
Hydrogen bonding.
Salt bonding.
Hemoglobin goes via the blood, heart, and muscle.
Myoglobin goes through (blood, heart, muscle) - ANSWER hemoglobin =
blood (RBCs)
Myoglobin = heart and muscle.
A protein that lacks its ligand or ligands - ANSWER apoprotein
(i.e., haemoglobin without heme)
a protein with its ligand that allows it to function - ANSWER haloprotein.
(i.e. hemoglobin is linked to heme).
What to know about heme - ANSWER 1. iron-containing pyrrole ring in the
center (for O2 binding).
2. it is regarded a prosthetic group (tightly attached to the globin)
Which has a higher oxygen affinity, myoglobin or hemoglobin?
