BCH210 Midterm Test 1| 160 Questions |
With Complete Solutions
proteins correct answer: polymers of amino acids linked in a
linear chain by peptide/amide bonds (polypeptides)
polysaccharides correct answer: polymers of sugars (mono-
saccharides) linked in linear and branched chains by glycosidic
bonds
DNA correct answer: polymers of nucleotides linked in linear
chains by phosphodiester bonds
protein enzymes correct answer: Linkages (bonds) are
formed/broken by _______?
sickle cell anemia correct answer: a single amino acid change in
hemoglobin protein; causes sickled red blood cells
dimerization correct answer: two things coming together
heterodimer correct answer: two polypeptide chains
non-covalent interactions correct answer: interactions that allow
binding and unbinding
covalent bonds correct answer: hold together amino acids; equal
electron sharing between two atoms
,non covalent bonds correct answer: allow chains to fold into
final structure
protein cofactors correct answer: non protein molecules and
metal ions that assist with protein structure and function; can
bound covalently or non covalently
transporters correct answer: bind molecules noncovalently
prosthetic groups correct answer: large chemicals that are
tightly bound by covalent or non-covalent forces
coenzyme correct answer: type of cofactor that 'shuttles'
commonly used functional groups in chemical reactions
metal ion cofactors correct answer: small molecules that
interact with protein and help with structure or be involved in
enzyme catalysis; perform noncovalent interactions
ionic/electrostatic interactions correct answer: strength depends
on polarity of charged species; sometimes known as salt bridge
for full +ve to -ve (charged) interactions
are important for ligand, cofactor, and/or substrate binding in
enzymes
salt bridges correct answer: a type of ionic interaction
can form between positively and negatively charged amino acids
,hydrogen bonds/bonding correct answer: strength is
proportional to polarity of H bond donor & acceptor; unequal
sharing between electronegative atom and H
strong, attractive non covalent forces; occur btwn molecules or
within parts of a single molecule
can form between hydroxyl, carboxyl, thiol, and amino groups
to help w protein solubility
can also form between amino acid side chains within a proteins
structure + backbone of polypeptides
hydrogen bond acceptors correct answer: electronegative atoms:
O, N, S, F, Cl, Br
hydrogen bond donors correct answer: hydrogen atoms
covalently bound to electronegative atoms
hydrophobic interactions correct answer: depends on entropy of
water being released, causing hydrophobic regions to come
together
can occur between aliphatic and hydrophobic side chains
van der waals forces correct answer: relatively weak + depends
on size of atoms and the distance between them; in non-polar
molecules and common in hydrophobic interactions
water correct answer: can form up to 4 transient hydrogen
bonds due to unequal sharing of electrons (dipole)
, excellent nucleophiles and can participate in hydrolysis and
condensation reactions
amphiphiles/amphipathic molecules correct answer: can be both
hydrophobic and hydrophilic
hydrophobic effect correct answer: nonpolar molecules
aggregate in an aqueous solution excl. water molecules;
tendency of water to avoid contact with non-polar molecules
(allows for macromolecular structures to form)
main driving force behind formation of macromolecular
structure/protein folding
excl. of water leads to INCREASE in entropy of water
molecules = obeys 2nd law of thermodynamics
agonist correct answer: a molecule that, by binding to a receptor
site, stimulates a response
hydrophilic acids; water correct answer: interaction of ______
with ______ helps solubilize proteins
amino acids correct answer: made up of an amino group (N-
terminus), carboxyl group (C-terminus), and an 'R' side chain
chirality correct answer: caused by asymmetric alpha carbon
centre
With Complete Solutions
proteins correct answer: polymers of amino acids linked in a
linear chain by peptide/amide bonds (polypeptides)
polysaccharides correct answer: polymers of sugars (mono-
saccharides) linked in linear and branched chains by glycosidic
bonds
DNA correct answer: polymers of nucleotides linked in linear
chains by phosphodiester bonds
protein enzymes correct answer: Linkages (bonds) are
formed/broken by _______?
sickle cell anemia correct answer: a single amino acid change in
hemoglobin protein; causes sickled red blood cells
dimerization correct answer: two things coming together
heterodimer correct answer: two polypeptide chains
non-covalent interactions correct answer: interactions that allow
binding and unbinding
covalent bonds correct answer: hold together amino acids; equal
electron sharing between two atoms
,non covalent bonds correct answer: allow chains to fold into
final structure
protein cofactors correct answer: non protein molecules and
metal ions that assist with protein structure and function; can
bound covalently or non covalently
transporters correct answer: bind molecules noncovalently
prosthetic groups correct answer: large chemicals that are
tightly bound by covalent or non-covalent forces
coenzyme correct answer: type of cofactor that 'shuttles'
commonly used functional groups in chemical reactions
metal ion cofactors correct answer: small molecules that
interact with protein and help with structure or be involved in
enzyme catalysis; perform noncovalent interactions
ionic/electrostatic interactions correct answer: strength depends
on polarity of charged species; sometimes known as salt bridge
for full +ve to -ve (charged) interactions
are important for ligand, cofactor, and/or substrate binding in
enzymes
salt bridges correct answer: a type of ionic interaction
can form between positively and negatively charged amino acids
,hydrogen bonds/bonding correct answer: strength is
proportional to polarity of H bond donor & acceptor; unequal
sharing between electronegative atom and H
strong, attractive non covalent forces; occur btwn molecules or
within parts of a single molecule
can form between hydroxyl, carboxyl, thiol, and amino groups
to help w protein solubility
can also form between amino acid side chains within a proteins
structure + backbone of polypeptides
hydrogen bond acceptors correct answer: electronegative atoms:
O, N, S, F, Cl, Br
hydrogen bond donors correct answer: hydrogen atoms
covalently bound to electronegative atoms
hydrophobic interactions correct answer: depends on entropy of
water being released, causing hydrophobic regions to come
together
can occur between aliphatic and hydrophobic side chains
van der waals forces correct answer: relatively weak + depends
on size of atoms and the distance between them; in non-polar
molecules and common in hydrophobic interactions
water correct answer: can form up to 4 transient hydrogen
bonds due to unequal sharing of electrons (dipole)
, excellent nucleophiles and can participate in hydrolysis and
condensation reactions
amphiphiles/amphipathic molecules correct answer: can be both
hydrophobic and hydrophilic
hydrophobic effect correct answer: nonpolar molecules
aggregate in an aqueous solution excl. water molecules;
tendency of water to avoid contact with non-polar molecules
(allows for macromolecular structures to form)
main driving force behind formation of macromolecular
structure/protein folding
excl. of water leads to INCREASE in entropy of water
molecules = obeys 2nd law of thermodynamics
agonist correct answer: a molecule that, by binding to a receptor
site, stimulates a response
hydrophilic acids; water correct answer: interaction of ______
with ______ helps solubilize proteins
amino acids correct answer: made up of an amino group (N-
terminus), carboxyl group (C-terminus), and an 'R' side chain
chirality correct answer: caused by asymmetric alpha carbon
centre
