Drexel bio 209 final Exam
comprehensive Questions With
Correct Verified And Well Analyzed
Answers Graded A+
weak interactions
electrostatic
h bonding
van der waals
hydrophobic effect- tendency of non polar molecules to avoid contact
with water in aqueous solutions
chemical bonds
strong- covalent (enzymes can change them)
weak/non covalent- protein folding, membranes, transport, substrate
binding
neg side chain amino acids
aspartic acid (Asp-D)
glutamic acid (Glu-E)
positive side chain amino acids
Arginine (Arg-R)
Lysine (Lys-K)
Histidine (His-H)
uncharged polar side chain
Asparagine (Asn-N)
Glutamine (Gln-Q)
Serine (Ser-S)
Threonine (Thr-T)
Tyrosine (Tyr-Y)
nonpolar amino acids
,alanine (ala- A)
glycine (gly-G)
valine (val-V)
leucine (leu-L)
isoleucine (ile-I)
proline (pro-P)
phenylalanine (phe-F)
methionine (met- M)
tryptophan (trp-W)
cytesine (cys-C)
all amino acids have
H atom
carboxyl group
amino group
Regroup (differentiating factor)
Linus Pauling and Robert Corey
X ray crystallography
- found alpha helix and beta pleated sheets (both interchain H
bonding)
bonds between each amino acid
peptide bond
amino acid chain= polypeptide backbone
polar and nonpolar amino acids face Opp sides in backbone
electrostatic interactions
between carboxyl and amino group of different amino acids
van der waals interactions
between methyl group off of side chains
alpha helix
tightly coiled
rod arrangement of amino acids
R-grop radiates outwards
backbone is repeating units of amino group bonded to carbonyl
group
,(n+4 rule)
3.6 amino acids per turn
right handed
a helix cont.
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
forms sheet by H bonding between amino and carboxyl groups of dif
peptide chains
parallel, antiparallel, mixed
extended polypeptide chains
levels of protein structure
primary- amino acid residues
secondary- alpha helix
tertiary- polypeptide chain
quaternary- assembled subunits
conservation of protein domains
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
polymer
ex. actin filaments
covalent bonds
disulfide bonds help stabilize protein structure
non covalent bonds
mediate specificity of binding between molecules
kinetic properties of enzymes
, 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
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
substrate bound within cleft
water excluded
nonpolar character enhances binding of substrate
enzyme substrate complex
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
ES complexes form until substrate saturation occurs at which point
no more substrate binding sites are available
reaction rates
enzymes increase reaction rate by decreasing activation energy
posttranslational regulation enzyme activity
allosteric regulation
covalent modification
proteolytic modification
allosteric regulation
feedback inhibition
regulates levels of synthesized end product
covalent modification
comprehensive Questions With
Correct Verified And Well Analyzed
Answers Graded A+
weak interactions
electrostatic
h bonding
van der waals
hydrophobic effect- tendency of non polar molecules to avoid contact
with water in aqueous solutions
chemical bonds
strong- covalent (enzymes can change them)
weak/non covalent- protein folding, membranes, transport, substrate
binding
neg side chain amino acids
aspartic acid (Asp-D)
glutamic acid (Glu-E)
positive side chain amino acids
Arginine (Arg-R)
Lysine (Lys-K)
Histidine (His-H)
uncharged polar side chain
Asparagine (Asn-N)
Glutamine (Gln-Q)
Serine (Ser-S)
Threonine (Thr-T)
Tyrosine (Tyr-Y)
nonpolar amino acids
,alanine (ala- A)
glycine (gly-G)
valine (val-V)
leucine (leu-L)
isoleucine (ile-I)
proline (pro-P)
phenylalanine (phe-F)
methionine (met- M)
tryptophan (trp-W)
cytesine (cys-C)
all amino acids have
H atom
carboxyl group
amino group
Regroup (differentiating factor)
Linus Pauling and Robert Corey
X ray crystallography
- found alpha helix and beta pleated sheets (both interchain H
bonding)
bonds between each amino acid
peptide bond
amino acid chain= polypeptide backbone
polar and nonpolar amino acids face Opp sides in backbone
electrostatic interactions
between carboxyl and amino group of different amino acids
van der waals interactions
between methyl group off of side chains
alpha helix
tightly coiled
rod arrangement of amino acids
R-grop radiates outwards
backbone is repeating units of amino group bonded to carbonyl
group
,(n+4 rule)
3.6 amino acids per turn
right handed
a helix cont.
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
forms sheet by H bonding between amino and carboxyl groups of dif
peptide chains
parallel, antiparallel, mixed
extended polypeptide chains
levels of protein structure
primary- amino acid residues
secondary- alpha helix
tertiary- polypeptide chain
quaternary- assembled subunits
conservation of protein domains
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
polymer
ex. actin filaments
covalent bonds
disulfide bonds help stabilize protein structure
non covalent bonds
mediate specificity of binding between molecules
kinetic properties of enzymes
, 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
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
substrate bound within cleft
water excluded
nonpolar character enhances binding of substrate
enzyme substrate complex
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
ES complexes form until substrate saturation occurs at which point
no more substrate binding sites are available
reaction rates
enzymes increase reaction rate by decreasing activation energy
posttranslational regulation enzyme activity
allosteric regulation
covalent modification
proteolytic modification
allosteric regulation
feedback inhibition
regulates levels of synthesized end product
covalent modification
