drexel bio 209 final EXAM fully solved & updated 2026(latest version verified
for accuracy) | 2026 Latest!!
weak interactions - (ANSWER)electrostatic
h bonding
van der waals
hydrophobic effect- tendency of non polar molecules to avoid contact with water in aqueous solutions
chemical bonds - (ANSWER)strong- covalent ( enzymes can change them)
weak/non covalent- protein folding, membranes, transport, substrate binding
neg side chain amino acids - (ANSWER)apartic acid(Asp-D)
glutamic acid (Glu-E)
positive side chain amino acids - (ANSWER)Arginine(Arg-R)
Lysine (Lys-K)
Histidine (His-H)
uncharged polar side chain - (ANSWER)Asparagine (Asn-N)
Glutamine (Gln-Q)
Serine (Ser-S)
Threosine (Thr-T)
Tyrosine (Tyr-Y)
nonpolar amino acids - (ANSWER)alanine (ala- A)
glycine (gly-G)
valine (val-V)
leucine (leu-L)
isoleucine (ile-I)
,drexel bio 209 final EXAM fully solved & updated 2026(latest version verified
for accuracy) | 2026 Latest!!
proline (pro-P)
phenylalanine (phe-F)
methionine (met- M)
tryptophan (trp-W)
cytesine (cys-C)
all amino acids have - (ANSWER)H atom
carboxyl group
amino group
Rgroup (differentiating factor)
Linus Pauling and Robert Corey - (ANSWER)X ray crystallography
- found alpha helix and beta pleated sheets (both interchain H bonding)
bonds between each amino acid - (ANSWER)peptide bond
amino acid chain= polypeptide backbone
polar and nonpolar amino acids face opp sides in backbone
electrostatic interactions - (ANSWER)between carboxyl and amino group of different amino acids
van der waals interactions - (ANSWER)between methyl group off of side chains
alpha helix - (ANSWER)tightly coiled
rod arrangement of amino acids
R-grop radiates outwards
backbone is repeating units of amino group bonded to carbonyl group
,drexel bio 209 final EXAM fully solved & updated 2026(latest version verified
for accuracy) | 2026 Latest!!
(n+4 rule)
3.6 amino acids per turn
right handed
a helix cont. - (ANSWER)two or more a helices intertwine to form coiled coil (ex. keratin, fibrin, myosin)
hemoglobin high in a helix content
chymotrypsin lacks a helix
b pleated sheet - (ANSWER)forms sheet by H bonding between amino and carboxyl groups of dif peptide
chains
parallel, antiparallel, mixed
extended polypeptide chains
levels of protein structure - (ANSWER)primary- amino acid residues
secondary- alpha helix
tertiary- polypeptide chain
quaternary- assembled subunits
conservation of protein domains - (ANSWER)humans and drosophilia share portions of the same amino
acid sequences
same protein domains can be found on different proteins
another name for protein assemblies - (ANSWER)polymer
ex. actin filaments
covalent bonds - (ANSWER)disulfide bonds help stabilize protein structure
, drexel bio 209 final EXAM fully solved & updated 2026(latest version verified
for accuracy) | 2026 Latest!!
non covalent bonds - (ANSWER)mediate specificity of binding between molecules
kinetic properties of enzymes - (ANSWER)increase rate of biological reaction without altering reaction
equilibria
decrease activation energy of a reaction
accelerate reactions through stabilization of transition states
the enzyme active site
enzyme active site - (ANSWER)the catalytic site is 3-d
substrates bound to enzyme by electrostatic, h bonding, van der waals forces, and hydrophobic
interactions
catalytic sites form clefts crevices - (ANSWER)substrate bound within cleft
water excluded
nonpolar character enhances binding of substrate
enzyme substrate complex - (ANSWER)x ray crystallography, electron microscope and
spectrophotometry
enzymes derive power by bringing in favorable substrate orientation
leonor michaelis: reaction rate increases with increasing s until vmax is achieved
saturation effect - (ANSWER)ES complexes form until substrate saturation occurs at which point no
more substrate binding sites are available
reaction rates - (ANSWER)enzymes increase reaction rate by decreasing activation energy
posttranslational regulation enzyme activity - (ANSWER)allosteric regulation
for accuracy) | 2026 Latest!!
weak interactions - (ANSWER)electrostatic
h bonding
van der waals
hydrophobic effect- tendency of non polar molecules to avoid contact with water in aqueous solutions
chemical bonds - (ANSWER)strong- covalent ( enzymes can change them)
weak/non covalent- protein folding, membranes, transport, substrate binding
neg side chain amino acids - (ANSWER)apartic acid(Asp-D)
glutamic acid (Glu-E)
positive side chain amino acids - (ANSWER)Arginine(Arg-R)
Lysine (Lys-K)
Histidine (His-H)
uncharged polar side chain - (ANSWER)Asparagine (Asn-N)
Glutamine (Gln-Q)
Serine (Ser-S)
Threosine (Thr-T)
Tyrosine (Tyr-Y)
nonpolar amino acids - (ANSWER)alanine (ala- A)
glycine (gly-G)
valine (val-V)
leucine (leu-L)
isoleucine (ile-I)
,drexel bio 209 final EXAM fully solved & updated 2026(latest version verified
for accuracy) | 2026 Latest!!
proline (pro-P)
phenylalanine (phe-F)
methionine (met- M)
tryptophan (trp-W)
cytesine (cys-C)
all amino acids have - (ANSWER)H atom
carboxyl group
amino group
Rgroup (differentiating factor)
Linus Pauling and Robert Corey - (ANSWER)X ray crystallography
- found alpha helix and beta pleated sheets (both interchain H bonding)
bonds between each amino acid - (ANSWER)peptide bond
amino acid chain= polypeptide backbone
polar and nonpolar amino acids face opp sides in backbone
electrostatic interactions - (ANSWER)between carboxyl and amino group of different amino acids
van der waals interactions - (ANSWER)between methyl group off of side chains
alpha helix - (ANSWER)tightly coiled
rod arrangement of amino acids
R-grop radiates outwards
backbone is repeating units of amino group bonded to carbonyl group
,drexel bio 209 final EXAM fully solved & updated 2026(latest version verified
for accuracy) | 2026 Latest!!
(n+4 rule)
3.6 amino acids per turn
right handed
a helix cont. - (ANSWER)two or more a helices intertwine to form coiled coil (ex. keratin, fibrin, myosin)
hemoglobin high in a helix content
chymotrypsin lacks a helix
b pleated sheet - (ANSWER)forms sheet by H bonding between amino and carboxyl groups of dif peptide
chains
parallel, antiparallel, mixed
extended polypeptide chains
levels of protein structure - (ANSWER)primary- amino acid residues
secondary- alpha helix
tertiary- polypeptide chain
quaternary- assembled subunits
conservation of protein domains - (ANSWER)humans and drosophilia share portions of the same amino
acid sequences
same protein domains can be found on different proteins
another name for protein assemblies - (ANSWER)polymer
ex. actin filaments
covalent bonds - (ANSWER)disulfide bonds help stabilize protein structure
, drexel bio 209 final EXAM fully solved & updated 2026(latest version verified
for accuracy) | 2026 Latest!!
non covalent bonds - (ANSWER)mediate specificity of binding between molecules
kinetic properties of enzymes - (ANSWER)increase rate of biological reaction without altering reaction
equilibria
decrease activation energy of a reaction
accelerate reactions through stabilization of transition states
the enzyme active site
enzyme active site - (ANSWER)the catalytic site is 3-d
substrates bound to enzyme by electrostatic, h bonding, van der waals forces, and hydrophobic
interactions
catalytic sites form clefts crevices - (ANSWER)substrate bound within cleft
water excluded
nonpolar character enhances binding of substrate
enzyme substrate complex - (ANSWER)x ray crystallography, electron microscope and
spectrophotometry
enzymes derive power by bringing in favorable substrate orientation
leonor michaelis: reaction rate increases with increasing s until vmax is achieved
saturation effect - (ANSWER)ES complexes form until substrate saturation occurs at which point no
more substrate binding sites are available
reaction rates - (ANSWER)enzymes increase reaction rate by decreasing activation energy
posttranslational regulation enzyme activity - (ANSWER)allosteric regulation
