BIOC384- Final Exam Set 4 UPDATED
ACTUAL Exam Questions and CORRECT
Answers
What is a difference between parallel and antiparallel beta-sheet secondary structures?
-Antiparallel beta-sheets have a larger number of stabilizing H bonds between backbone amides
than parallel beta-sheets.
-Parallel beta-sheets require a larger loop connecting together the individual peptide strands in
the sheet.
-Parallel beta-sheets are longer than antiparallel sheets.
-Parallel beta-sheets have amino acid side chains alternating up and down, whereas antiparallel
side chains alternate down and up. - CORRECT ANSWER - Parallel beta-sheets require a
larger loop connecting together the individual peptide strands in the sheet.
How many beta-turns or beta-loops are required to construct a beta-sheet composed of four
antiparallel strands?
0
3
4
5 - CORRECT ANSWER -3
Which class of protein structures does the protein shown below fit into?
predominantly alpha-helical
predominantly beta-sheet
intermixed alpha-helix and beta-sheet
domains of alpha-helix adjacent to domains of beta-sheet - CORRECT ANSWER -
predominantly beta-sheet
, The common protein fold shown below is the __________ fold.
Greek key
Rossman
FERM domain
alpha/beta barrel - CORRECT ANSWER - alpha/beta barrel
The protein fold known as the Rossman fold is found in proteins that commonly bind
alpha-helices.
nucleotides.
cytochromes.
membranes. - CORRECT ANSWER - nucleotides.
Protein tertiary structures
-require the formation of disulfide bonds in order to achieve their native state.
-are always irreversibly destroyed by the addition of denaturants, such as urea and salts, even
when the denaturants are subsequently removed.
-are often disrupted by the either very low pH or very high pH values as a result of alterations in
the ionization states of acidic or basic amino acids.
-are generally poorly defined and cannot be determined experimentally. - CORRECT
ANSWER - are often disrupted by the either very low pH or very high pH values as a
result of alterations in the ionization states of acidic or basic amino acids.
At the interface between subunits of a protein with quaternary structure, which of the following
interactions between amino acid side chains would contribute to the stability of the dimer?
glutamate-aspartate.
ACTUAL Exam Questions and CORRECT
Answers
What is a difference between parallel and antiparallel beta-sheet secondary structures?
-Antiparallel beta-sheets have a larger number of stabilizing H bonds between backbone amides
than parallel beta-sheets.
-Parallel beta-sheets require a larger loop connecting together the individual peptide strands in
the sheet.
-Parallel beta-sheets are longer than antiparallel sheets.
-Parallel beta-sheets have amino acid side chains alternating up and down, whereas antiparallel
side chains alternate down and up. - CORRECT ANSWER - Parallel beta-sheets require a
larger loop connecting together the individual peptide strands in the sheet.
How many beta-turns or beta-loops are required to construct a beta-sheet composed of four
antiparallel strands?
0
3
4
5 - CORRECT ANSWER -3
Which class of protein structures does the protein shown below fit into?
predominantly alpha-helical
predominantly beta-sheet
intermixed alpha-helix and beta-sheet
domains of alpha-helix adjacent to domains of beta-sheet - CORRECT ANSWER -
predominantly beta-sheet
, The common protein fold shown below is the __________ fold.
Greek key
Rossman
FERM domain
alpha/beta barrel - CORRECT ANSWER - alpha/beta barrel
The protein fold known as the Rossman fold is found in proteins that commonly bind
alpha-helices.
nucleotides.
cytochromes.
membranes. - CORRECT ANSWER - nucleotides.
Protein tertiary structures
-require the formation of disulfide bonds in order to achieve their native state.
-are always irreversibly destroyed by the addition of denaturants, such as urea and salts, even
when the denaturants are subsequently removed.
-are often disrupted by the either very low pH or very high pH values as a result of alterations in
the ionization states of acidic or basic amino acids.
-are generally poorly defined and cannot be determined experimentally. - CORRECT
ANSWER - are often disrupted by the either very low pH or very high pH values as a
result of alterations in the ionization states of acidic or basic amino acids.
At the interface between subunits of a protein with quaternary structure, which of the following
interactions between amino acid side chains would contribute to the stability of the dimer?
glutamate-aspartate.
