BCH210 midterm Questions
With Complete Solutions
identify all the polar amino acids correct answer: cysteine (cys),
asparatate (asp), glutamate (glu), histidine (his) , lysine (lys),
asparagine (asn), arginine (arg), serine (ser), threonine (thr), and
glutamine (gln)
identify all the nonpolar (hydrophobic) amino acids correct
answer: alanine (ala), proline (pro), phenylalanine (phe), valine
(val), leucine (leu), and isoleucine (ile)
identify all of the amphipathic/mixed properties amino acids:
correct answer: methionine (met), tyrosine (tyr), glycine (gly),
and tryptophan (trp)
tryptophan, although it is argued whether polar or nonpolar is...
correct answer: mostly hydrophobic
methionine, although it is argued whether polar or nonpolar is...
correct answer: is mostly polar
List all the aromatic amino acids correct answer: phenylalanine,
tyrosine, tryptophan
proteins play a variety of roles including... correct answer:
catalysis, structure, recognition (binding to certain things)
,hemoglobin plays a role in what? correct answer: oxygen
transport
sucrose uses h2o to what? correct answer: to break down into
glucose and fructose
what are glycoproteins correct answer: proteins with sugars
attached
what type of bonds hold together amino acids? correct answer:
covalent bonds (peptide bonds)
what type of bonds allow a peptide chain to fold into its final
structure? correct answer: non-covalent bonds
cofactors are bonded... correct answer: covalently or non-
covalently
transporter proteins are bonded... correct answer: non-
covalently
what is a protein cofactor? correct answer: any non-protein
molecule or metal ion that'll help the protein adapt its final
structure or function
what are prosthetic groups? correct answer: similar to cofactors,
but they are bound to the enzyme, rather than being separate
molecules or atoms
How are prosthetic groups bound? correct answer: tightly,
covalently or non-covalently
,what are coenzymes? correct answer: organic cofactors that
serve as "shuttles" for commonly-used functional groups in
chemical reactions (vitamins)
what is an example of a metal ion cofactor? correct answer:
calmodulin
- requires Ca2+ to get its final structure (no binding interface
without Ca2+
what are the strongest type of bonds? correct answer: covalent
what are the longest type of bonds? correct answer: van der
waals (also the weakes)
how many functional groups can be hydrogen donors? correct
answer: 7 (hydroxyl, carboxyl, amine, thiol, amide, phosphate
and imidazole)
how many functional groups can be acceptors? correct answer:
11
what is the hydrophobic effect? correct answer: the observed
tendency of nonpolar substances to aggregate in aqueous
solution and exclude water molecules
what happens to entropy during the hydrophobic effect? correct
answer: - entropy of the hydrophobic structure decreases
- entropy of the solution (water molecules) increases
, what is a reason as to why proteins fold? correct answer: - don't
want water to cleave all the peptide bonds in a structure
amino acids are made up of what three components? correct
answer: - amino group
- carboxyl group
- "R" side xhain
what does it mean when an amino acid is essential? Non-
essential? correct answer: essential: must be obtained from diet
non-essential: already in our bodies
what are the only 6 letters non representing amino acids? correct
answer: JUZ BOX
in an amino acid, which carbon is the the primary carbon? which
is the secondary carbon? correct answer: primary carbon:
carbon on the carboxyl
secondary: α-carbon
what does it mean for a structure to be chiral? correct answer:
asymmetry; a carbon with 4 different groups attatched
what are enantiomers? correct answer: non-superimposable
mirror images
Which isomer of amino acids is most commonly used in
biological systems? correct answer: L-isomer
what is a zwitterion? correct answer: a neutral molecule that has
separate positive and negative charged functional groups
With Complete Solutions
identify all the polar amino acids correct answer: cysteine (cys),
asparatate (asp), glutamate (glu), histidine (his) , lysine (lys),
asparagine (asn), arginine (arg), serine (ser), threonine (thr), and
glutamine (gln)
identify all the nonpolar (hydrophobic) amino acids correct
answer: alanine (ala), proline (pro), phenylalanine (phe), valine
(val), leucine (leu), and isoleucine (ile)
identify all of the amphipathic/mixed properties amino acids:
correct answer: methionine (met), tyrosine (tyr), glycine (gly),
and tryptophan (trp)
tryptophan, although it is argued whether polar or nonpolar is...
correct answer: mostly hydrophobic
methionine, although it is argued whether polar or nonpolar is...
correct answer: is mostly polar
List all the aromatic amino acids correct answer: phenylalanine,
tyrosine, tryptophan
proteins play a variety of roles including... correct answer:
catalysis, structure, recognition (binding to certain things)
,hemoglobin plays a role in what? correct answer: oxygen
transport
sucrose uses h2o to what? correct answer: to break down into
glucose and fructose
what are glycoproteins correct answer: proteins with sugars
attached
what type of bonds hold together amino acids? correct answer:
covalent bonds (peptide bonds)
what type of bonds allow a peptide chain to fold into its final
structure? correct answer: non-covalent bonds
cofactors are bonded... correct answer: covalently or non-
covalently
transporter proteins are bonded... correct answer: non-
covalently
what is a protein cofactor? correct answer: any non-protein
molecule or metal ion that'll help the protein adapt its final
structure or function
what are prosthetic groups? correct answer: similar to cofactors,
but they are bound to the enzyme, rather than being separate
molecules or atoms
How are prosthetic groups bound? correct answer: tightly,
covalently or non-covalently
,what are coenzymes? correct answer: organic cofactors that
serve as "shuttles" for commonly-used functional groups in
chemical reactions (vitamins)
what is an example of a metal ion cofactor? correct answer:
calmodulin
- requires Ca2+ to get its final structure (no binding interface
without Ca2+
what are the strongest type of bonds? correct answer: covalent
what are the longest type of bonds? correct answer: van der
waals (also the weakes)
how many functional groups can be hydrogen donors? correct
answer: 7 (hydroxyl, carboxyl, amine, thiol, amide, phosphate
and imidazole)
how many functional groups can be acceptors? correct answer:
11
what is the hydrophobic effect? correct answer: the observed
tendency of nonpolar substances to aggregate in aqueous
solution and exclude water molecules
what happens to entropy during the hydrophobic effect? correct
answer: - entropy of the hydrophobic structure decreases
- entropy of the solution (water molecules) increases
, what is a reason as to why proteins fold? correct answer: - don't
want water to cleave all the peptide bonds in a structure
amino acids are made up of what three components? correct
answer: - amino group
- carboxyl group
- "R" side xhain
what does it mean when an amino acid is essential? Non-
essential? correct answer: essential: must be obtained from diet
non-essential: already in our bodies
what are the only 6 letters non representing amino acids? correct
answer: JUZ BOX
in an amino acid, which carbon is the the primary carbon? which
is the secondary carbon? correct answer: primary carbon:
carbon on the carboxyl
secondary: α-carbon
what does it mean for a structure to be chiral? correct answer:
asymmetry; a carbon with 4 different groups attatched
what are enantiomers? correct answer: non-superimposable
mirror images
Which isomer of amino acids is most commonly used in
biological systems? correct answer: L-isomer
what is a zwitterion? correct answer: a neutral molecule that has
separate positive and negative charged functional groups
