M2P
Exam
1
Questions
with
100%
Correct
Answers
|
Latest
Update
2024
|
Verified
Types
of
Proteins
-
ANSWER-o
Cellular
/
nuclear
o
Integral
membrane,
membrane-anchored,
membrane-attached
o
Extracellular
/
secreted
Examples
of
proteins
-
ANSWER-Collagen,
Hormones,
Receptors
-
cell
surface/nuclear,
Enzymes,
Transporters,
Channels,
Cytoskeleton,
Motor
proteins
/
transport,
Antibodies,
Neuropeptides,
Transcription
factors,
Chaperones,
Histones,
Binding
proteins
primary
protein
structure
-
ANSWER-Linear
sequence
of
amino
acid
residues
joined
through
peptide
bonds
to
form
a
polypeptide
chain:
-Peptide
bonds
between
adjacent
amino
acids
-Covalent
bond
b/w
carboxyl
of
one
and
amino
of
other
that
requires
energy
and
condensation
rxn
with
a
release
of
a
water
molecule
-carbonyl
&
amide
of
peptide
bond
exhibit
strong
electronegativity
-
Side
chains
exist
in
trans
configuration
to
prevent
steric
hindrance
-Limits
secondary
and
tertiary
structures
that
can
be
formed
from
the
polypeptide
chain.
-Resonance
due
to
electron
delocalization
secondary
protein
structure
-
ANSWER-·
recurring
structures
(e.g.,
the
regular
structure
of
the
α-
helix)
that
form
in
short
localized
regions
of
the
polypeptide
chain
o
HYDROGEN
BONDS-
stabilize
this
structure
-2
types:
alpha
and
beta
peptide
bond
-
ANSWER-The
chemical
bond
that
forms
between
the
carboxyl
group
of
one
amino
acid
and
the
amino
group
of
another
amino
acid
(IN
PRIMARY
STRUCTURE) -restrictive
due
to
RESONANCE
Limited
conformational
states
of
a
polypeptide
-planar
with
little
bond
rotation
Alpha
Helices
-
ANSWER-_-type
of
protein
secondary
structure
-Stabilized
by
hydrogen
bonds
parallel
to
helix
axis
-R
groups
project
radially
outward
-can
be
right-handed
or
left-handed.
-An
amphipathic
α-
helix
may
be
located
at
protein
surface;
hydrophilic
R-groups
project
out
into
solvent
&
hydrophobic
R-groups
project
inward
to
protein
core
Beta
sheet
-
ANSWER--Type
of
Secondary
protein
structure
-stabilized
by
hydrogen
bonds
co-planar
with
β-
pleat
-hydrogen
bonds
in
different
regions
of
the
polypeptide
-R
groups
alternately
project
above
&
below
plane
of
the
sheet
-stabilized
by
a
single
hydrogen
bond
between
AA1
and
AA4
-3
types:
parallel,
antiparallel,
mixed
Parallel
Beta
Sheets
-
ANSWER--Type
of
beta
sheet
protein
secondary
structure
-start
and
end
with
same
terminus,
N
matches
with
N
and
C
matches
with
C
-Occurs
between
neighboring,
different
polypeptide
chains
-Hydrogen
bonding
between
two
chains
is
slightly
skewed
antiparallel
beta
sheet
-
ANSWER--Type
of
beta
sheet
protein
secondary
structure
-
mismatch
N
and
C
terminus
-Hydrogen
bonding
between
two
chains
is
directly
across
-Occur
within
same
polypeptide
chain,
facilitated
by
hairpin
loop
-HAIRPIN-
proline
(facilitates
sharp
turn
of
loop,
due
to
ring
R
group),
glycine
(
in
third
position,
lacks
R
group
so
it
doesn't
have
steric
hinderance
with
proline)
Mixed
Beta
sheets
-
ANSWER-
super
secondary
protein
structure
-
ANSWER--Pattern
of
secondary
structure
elements
recognized
in
multiple
proteins=
motif
-Ex.
βα
β
structural
motif
(Most
common)
α-
helix
connects
two
parallel
β-
sheets -Includes
nonrepetitive
structures
(turns,
coils,
and
loops-
like
hairpin
loops)
-NOT
random
Tertiary
Protein
structure
-
ANSWER--the
overall
three-dimensional
conformation,
the
summation
of
its
secondary
structural
elements
-Lots
of
energy
in
ATP
required
from
ATP
hydrolysis
-Chaperone
proteins
(heat
shock
proteins)
protect
and
assist
in
proper
protein
folding-
prevent
polypeptide
chain
degradation
or
wrong
rxns
occurring:
-Native
conformation-
final
folded
form
of
the
polypeptide
in
3D
form
-Several
Interactions:
Stabilized
by
hydrophobic
interactions
(aromatic
amino
acids),
hydrogen
bonds,
ionic
interactions
(acidic/basic
amino
acids),
disulfide
bonds
(sulfhydral-containing
amino
acids)
-Creates
specific
and
flexible
binding
sites
for
ligands
-Has
to
exist
in
environment
without
losing
structure
-Maintains
appropriate
surface
for
the
protein's
cellular
location
-Examples:
Myoglobin
and
G-actin
-Typically
comprised
of
one
or
more
super-secondary
structure
quartenary
protein
structure
-
ANSWER-is
the
association
of
polypeptide
subunits
in
a
geometrically
specific
manner
-Most
complex
level
-Multiple
polypeptide
chains
(subunits)
assembled
into
a
supra-molecular
complex
-Ex.
Hemoglobbin-
4
subunits,
tetramer,
two
beta
and
two
alpha
-Number
of
subunits
designated
by
suffix,
i.e.,
dimeric
(2),
trimeric
(3),
etc.
-May
consist
of
identical
(homopolymeric)
or
different
(heteropolymeric)
subunits
The
hsp
70
family
chaperone
proteins
-
ANSWER--type
of
chaperone
and
heat-shock
protein
-prevents
folding
of
the
nascent
chain
and
promote
unfolding.
The
ATPase
domain
of
the
protein
has
the
actin
fold.
This
figure
depicts
the
synthesis
of
protein
from
ribosomes
bound
to
mRNA
in
the
cytoplasm
The
hsp
60
Class
of
chaperone
proteins
-
ANSWER--type
of
chaperone
and
heat-shock
protein
Exam
1
Questions
with
100%
Correct
Answers
|
Latest
Update
2024
|
Verified
Types
of
Proteins
-
ANSWER-o
Cellular
/
nuclear
o
Integral
membrane,
membrane-anchored,
membrane-attached
o
Extracellular
/
secreted
Examples
of
proteins
-
ANSWER-Collagen,
Hormones,
Receptors
-
cell
surface/nuclear,
Enzymes,
Transporters,
Channels,
Cytoskeleton,
Motor
proteins
/
transport,
Antibodies,
Neuropeptides,
Transcription
factors,
Chaperones,
Histones,
Binding
proteins
primary
protein
structure
-
ANSWER-Linear
sequence
of
amino
acid
residues
joined
through
peptide
bonds
to
form
a
polypeptide
chain:
-Peptide
bonds
between
adjacent
amino
acids
-Covalent
bond
b/w
carboxyl
of
one
and
amino
of
other
that
requires
energy
and
condensation
rxn
with
a
release
of
a
water
molecule
-carbonyl
&
amide
of
peptide
bond
exhibit
strong
electronegativity
-
Side
chains
exist
in
trans
configuration
to
prevent
steric
hindrance
-Limits
secondary
and
tertiary
structures
that
can
be
formed
from
the
polypeptide
chain.
-Resonance
due
to
electron
delocalization
secondary
protein
structure
-
ANSWER-·
recurring
structures
(e.g.,
the
regular
structure
of
the
α-
helix)
that
form
in
short
localized
regions
of
the
polypeptide
chain
o
HYDROGEN
BONDS-
stabilize
this
structure
-2
types:
alpha
and
beta
peptide
bond
-
ANSWER-The
chemical
bond
that
forms
between
the
carboxyl
group
of
one
amino
acid
and
the
amino
group
of
another
amino
acid
(IN
PRIMARY
STRUCTURE) -restrictive
due
to
RESONANCE
Limited
conformational
states
of
a
polypeptide
-planar
with
little
bond
rotation
Alpha
Helices
-
ANSWER-_-type
of
protein
secondary
structure
-Stabilized
by
hydrogen
bonds
parallel
to
helix
axis
-R
groups
project
radially
outward
-can
be
right-handed
or
left-handed.
-An
amphipathic
α-
helix
may
be
located
at
protein
surface;
hydrophilic
R-groups
project
out
into
solvent
&
hydrophobic
R-groups
project
inward
to
protein
core
Beta
sheet
-
ANSWER--Type
of
Secondary
protein
structure
-stabilized
by
hydrogen
bonds
co-planar
with
β-
pleat
-hydrogen
bonds
in
different
regions
of
the
polypeptide
-R
groups
alternately
project
above
&
below
plane
of
the
sheet
-stabilized
by
a
single
hydrogen
bond
between
AA1
and
AA4
-3
types:
parallel,
antiparallel,
mixed
Parallel
Beta
Sheets
-
ANSWER--Type
of
beta
sheet
protein
secondary
structure
-start
and
end
with
same
terminus,
N
matches
with
N
and
C
matches
with
C
-Occurs
between
neighboring,
different
polypeptide
chains
-Hydrogen
bonding
between
two
chains
is
slightly
skewed
antiparallel
beta
sheet
-
ANSWER--Type
of
beta
sheet
protein
secondary
structure
-
mismatch
N
and
C
terminus
-Hydrogen
bonding
between
two
chains
is
directly
across
-Occur
within
same
polypeptide
chain,
facilitated
by
hairpin
loop
-HAIRPIN-
proline
(facilitates
sharp
turn
of
loop,
due
to
ring
R
group),
glycine
(
in
third
position,
lacks
R
group
so
it
doesn't
have
steric
hinderance
with
proline)
Mixed
Beta
sheets
-
ANSWER-
super
secondary
protein
structure
-
ANSWER--Pattern
of
secondary
structure
elements
recognized
in
multiple
proteins=
motif
-Ex.
βα
β
structural
motif
(Most
common)
α-
helix
connects
two
parallel
β-
sheets -Includes
nonrepetitive
structures
(turns,
coils,
and
loops-
like
hairpin
loops)
-NOT
random
Tertiary
Protein
structure
-
ANSWER--the
overall
three-dimensional
conformation,
the
summation
of
its
secondary
structural
elements
-Lots
of
energy
in
ATP
required
from
ATP
hydrolysis
-Chaperone
proteins
(heat
shock
proteins)
protect
and
assist
in
proper
protein
folding-
prevent
polypeptide
chain
degradation
or
wrong
rxns
occurring:
-Native
conformation-
final
folded
form
of
the
polypeptide
in
3D
form
-Several
Interactions:
Stabilized
by
hydrophobic
interactions
(aromatic
amino
acids),
hydrogen
bonds,
ionic
interactions
(acidic/basic
amino
acids),
disulfide
bonds
(sulfhydral-containing
amino
acids)
-Creates
specific
and
flexible
binding
sites
for
ligands
-Has
to
exist
in
environment
without
losing
structure
-Maintains
appropriate
surface
for
the
protein's
cellular
location
-Examples:
Myoglobin
and
G-actin
-Typically
comprised
of
one
or
more
super-secondary
structure
quartenary
protein
structure
-
ANSWER-is
the
association
of
polypeptide
subunits
in
a
geometrically
specific
manner
-Most
complex
level
-Multiple
polypeptide
chains
(subunits)
assembled
into
a
supra-molecular
complex
-Ex.
Hemoglobbin-
4
subunits,
tetramer,
two
beta
and
two
alpha
-Number
of
subunits
designated
by
suffix,
i.e.,
dimeric
(2),
trimeric
(3),
etc.
-May
consist
of
identical
(homopolymeric)
or
different
(heteropolymeric)
subunits
The
hsp
70
family
chaperone
proteins
-
ANSWER--type
of
chaperone
and
heat-shock
protein
-prevents
folding
of
the
nascent
chain
and
promote
unfolding.
The
ATPase
domain
of
the
protein
has
the
actin
fold.
This
figure
depicts
the
synthesis
of
protein
from
ribosomes
bound
to
mRNA
in
the
cytoplasm
The
hsp
60
Class
of
chaperone
proteins
-
ANSWER--type
of
chaperone
and
heat-shock
protein
