Kaplan Chapter 3 Nonenzymatic Protein Function and Protein Analysis Flashcards

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1
Q

What are Structural protein

A

They are composed of the cytoskeleton, anchoring proteins,
and much of the extracellular matrix.

The most common structural proteins are collagen, elastin, and tubulin

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2
Q

What is collagen?

A

Collagen is the most abundant structural protein in the body, providing strength and support to tissues like skin, bones, and tendons. Its synthesis requires vitamin C, and defects in collagen production can lead to conditions like scurvy or osteogenesis imperfecta. Collagen comes in different types (e.g., Type I in bones and skin, Type II in cartilage), each serving specific functions in maintaining tissue integrity.

Key word: Strength and Flexibility

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3
Q

What is elastin?

A

Elastin is a key structural protein that gives tissues like skin, lungs, and blood vessels their elasticity, allowing them to stretch and return to their original shape. It is primarily found in connective tissues and works alongside collagen to provide both flexibility and strength. Defects in elastin can lead to conditions like emphysema and Marfan syndrome, which affect the elasticity of tissues.

Key word: Restores original shape of Tissue

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4
Q

What is keratin?

A

Keratin Summary:
Keratin is a tough, fibrous structural protein found in hair, nails, and the outer layer of skin, providing protection and mechanical strength. It is highly resistant to wear and tear, contributing to the body’s barrier against physical and environmental damage. Keratin also forms in epithelial cells in the lining of various organs and tissues.

MCAT Relevance:
Keratin is relevant to the MCAT in questions related to epithelial tissue function, structural proteins, and the body’s protective barriers. It’s also important for understanding the differences between various structural proteins like keratin, collagen, and elastin, as well as disorders related to skin and hair.

Key word: mechanical integrity and regulatory proteins.

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5
Q

What is tubulin?

A

Tubulin Summary:
Tubulin is a globular protein that forms microtubules, which are essential components of the cytoskeleton. Microtubules provide structural support, aid in intracellular transport, and are crucial for cell division, particularly in the formation of the mitotic spindle.

MCAT Relevance:
Tubulin is important for the MCAT in topics involving cell structure and function, mitosis/meiosis, and intracellular transport mechanisms. Questions may cover the role of tubulin in processes like chromosome separation during cell division, cilia and flagella movement, and the impact of drugs (e.g., taxol) that target tubulin in cancer therapy.

Key word: provide structure, chromosome seperation in mitosis, intracellular transport with kinesin …
- end by nucleus
+ end by the outside

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6
Q

What are motor protiens?

A

Motor proteins have one or more heads capable of force generation through a conformational change.

They have catalytic activity, acting as ATPases to power movement.

Muscle contraction, vesicle movement within cells, and cell motility are the most common applications of motor proteins.

Common examples include myosin, kinesin, and dynein.

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7
Q

What is ATPase and what does it do?

A

ATPase Summary:
ATPase is an enzyme that catalyzes the hydrolysis of ATP into ADP and inorganic phosphate, releasing energy for various cellular processes. It plays a key role in active transport, muscle contraction, and maintaining ion gradients across membranes (e.g., the Na⁺/K⁺ pump).

MCAT Relevance:
ATPase is crucial for the MCAT in topics like cellular energy metabolism, active transport, and muscle physiology. Questions may focus on ATPase’s role in maintaining ion gradients, driving processes like nerve impulses, and its function in muscle contraction through the interaction with actin and myosin.

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8
Q

What is a binding protein?

A

Binds a specific substrate, either to sequester it in the
body or hold its concentration at steady state.

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9
Q

What is cell adhesion Molecules?

A

CAM bind a specific substrate, either to sequester it in the
body or hold its concentration at steady state.

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10
Q

What is myosin?

A

Myosin Summary:
Myosin is a motor protein that interacts with actin filaments to facilitate muscle contraction and various cellular movements. It converts chemical energy from ATP hydrolysis into mechanical work, enabling processes like muscle contraction and intracellular transport.

MCAT Relevance:
Myosin is important for the MCAT in muscle physiology, cellular movement, and protein function. Questions might cover its role in muscle contraction (e.g., the sliding filament theory), its interaction with actin, and its function in other cellular processes like cytokinesis and vesicle transport.

Has a thicc neck which is responsible for the power strike of a saccromere contraction.

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11
Q

What is Kinesins and Dyneins?

A

Kinesins and Dyneins Summary:
Kinesins and dyneins are motor proteins that transport cellular components along microtubules. Kinesins generally move toward the plus end of microtubules (outward from the cell center), while dyneins move toward the minus end (toward the cell center).

MCAT Relevance:
Kinesins and dyneins are important for the MCAT in topics related to intracellular transport, cytoskeleton function, and cell division. Questions may cover their roles in moving organelles, vesicles, and other cargo within cells, as well as their involvement in processes like mitosis and cellular organization.

Importance: has 2 heads, 1 attached to Metaphase, both are important during metaphase for vesicle transoprt/

Dyneiens are involved in the movement of cilia and flagella.

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11
Q

What is Cadherins?

A

A type of binding protein that are calcium-dependent glycoproteins that hold similar
cells together.

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12
Q

What are Integrins?

A

A type of binding protein
that have two membrane-spanning chains and permit cells to adhere to proteins in the extracellular matrix. Some also have signaling capabilities.

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13
Q

What are selectins?

A

A type of binding protein
that carbohydrates on the surfaces of other cells and are most commonly used in the immune system

Selectins are relevant for the MCAT in cellular adhesion, immune response, and inflammation. Questions might address their role in leukocyte trafficking, their function in the inflammatory response, and how selectins interact with other adhesion molecules to mediate cell movement and immune cell recruitmen

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14
Q

What are Antibodies (or immunoglobulins, Ig)

A

Antibodies (or immunoglobulins, Ig) are used by the immune
system to target a specific antigen, which may be a protein on the
surface of a pathogen (invading organism) or a toxin.

Immunoglobulins contain a constant region and a variable region;
the variable region is responsible for antigen binding.

Two identical heavy chains and two identical light chains form a
single antibody; they are held together by disulfide linkages and
noncovalent interactions.

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15
Q

What is Biosignaling?

A

Biosignaling is a process in which cells receive and act on signals. Proteins
participate in biosignaling in different capacities, including acting as
extracellular ligands, transporters for facilitated diffusion, receptor proteins,
and second messengers. e proteins involved in biosignaling can have
functions in substrate binding or enzymatic activity

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16
Q

What are Ion Channels used for?

A

Ion channels can be used for regulating ion flow into or out of a cell.
There are three main types of ion channels: Ungated channels, Voltage-gated channels, Ligand-gated channels

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17
Q

What are Ungated channels?

A

Ungated channels, also known as leak channels, are ion channels that are always open, allowing ions to flow across the cell membrane freely. They contribute to the resting membrane potential and help maintain ion gradients within the cell.

MCAT Relevance:
Ungated channels are relevant for the MCAT in neurophysiology, cell membrane function, and electrophysiology. Questions may cover their role in maintaining the resting membrane potential, their contribution to the passive movement of ions, and their impact on cellular excitability and signaling.

ALWAYS OPEN

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18
Q

What are Voltage-gated channels?

A

Voltage-Gated Channels Summary:
Voltage-gated channels are a type of Ion Channel that open or close in response to changes in membrane potential. They are crucial for generating and propagating action potentials in neurons and muscle cells, as they allow ions to flow across the membrane in a controlled manner.

MCAT Relevance:
Voltage-gated channels are important for the MCAT in topics related to neurophysiology, action potentials, and cellular excitability. Questions may focus on their role in the depolarization and repolarization phases of action potentials, their specific ion selectivity (e.g., sodium or potassium channels), and their function in the propagation of electrical signals along nerves and muscles.

are open within a range of membrane potentials.

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19
Q

What are Ligand-gated channels?

A

Ligand-Gated Channels Summary:
Ligand-gated channels are a type of Ion Channel that open in response to the binding of a specific molecule, such as a hormone or neurotransmitter. This binding causes a conformational change in the channel, allowing ions to flow across the membrane and initiate cellular responses.

MCAT Relevance:
Ligand-gated channels are relevant for the MCAT in topics related to cell signaling, synaptic transmission, and neurophysiology. Questions may address their role in neurotransmission, the mechanisms of signal transduction, and how ligand binding influences channel activity to affect cellular functions.

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20
Q

What are Enzyme-Linked Receptors

A

Enzyme-Linked Receptors Summary:
Enzyme-linked receptors are membrane proteins with three main domains: a membrane-spanning domain, a ligand-binding domain, and a catalytic domain. When a ligand binds to the receptor, it induces a conformational change that activates the catalytic domain, leading to a cascade of biochemical events inside the cell. Examples include receptor tyrosine kinases (RTKs), which dimerize and autophosphorylate upon ligand binding, initiating further signaling.

MCAT Relevance:
Enzyme-linked receptors are key in cell signaling and signal transduction pathways. Questions may focus on their structure, activation mechanism, and the role of RTKs and other enzyme-linked receptors in cellular processes. Understanding these mechanisms is crucial for topics related to cellular responses and intracellular signaling cascades.

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21
Q

What are G Protein-Coupled Receptors (GPCRs)

A

G Protein-Coupled Receptors (GPCRs) Summary:
GPCRs are integral membrane proteins with seven α-helical segments that facilitate signal transduction. They operate through a trimeric G protein complex consisting of α, β, and γ subunits. Ligand binding to a GPCR activates the associated G protein by exchanging GDP for GTP on the α subunit, which then dissociates from the β and γ subunits. The activated α subunit influences downstream effectors like adenylate cyclase or phospholipase C, leading to changes in second messenger levels. The α subunit eventually hydrolyzes GTP to GDP, re-associating with the β and γ subunits, and returning to its inactive state.

MCAT Relevance:
GPCRs are crucial for understanding cell signaling pathways, receptor mechanisms, and pharmacology. Questions might focus on the GPCR structure, the process of G protein activation, the role of different G protein types (Gs, Gi, Gq), and the impact on second messenger systems such as cAMP or IP3/DAG. Understanding these concepts is essential for comprehending how cells respond to various stimuli and how drugs can influence these pathways.

G protein-coupled receptors have a membrane-bound protein associated with a trimeric G protein. They also initiate second messenger systems.
Ligand binding engages the G protein. GDP is replaced with GTP; the α subunit dissociates from the β and
γ subunits. The activated α subunit alters the activity of adenylate cyclase or
phospholipase C. GTP is dephosphorylated to GDP; the α subunit rebinds to the β and γ subunits.

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22
Q

What is Electrophoresis?

A

Electrophoresis uses a gel matrix to observe the migration of proteins
in response to an electric field.

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23
Q

What is Native PAGE?

A

Native PAGE maintains the protein’s shape, but results are difficult
to compare because the mass-to-charge ratio differs for each
protein

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24
Q

What is SDS-PAGE?

A

SDS-PAGE denatures the proteins and masks the native charge so
that comparison of size is more accurate, but the functional protein
cannot be recaptured from the gel.

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25
Q

What is Isoelectric focusing?

A

Isoelectric focusing separates proteins by their isoelectric point (pI); the protein migrates toward an electrode until it reaches a
region of the gel where pH = pI of the protein.

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26
Q

What is X-ray
crystallography used for?

A

Protein structure is primarily determined through X-ray crystallography aer the protein is isolated, although NMR can also
be used.

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27
Q

How is Amino acid composition determined?

A

Amino acid composition can be determined by simple hydrolysis, but
amino acid sequencing requires sequential degradation, such as the
Edman degradation. [The Edman degradation selectively and sequentially
removes the N-terminal amino acid of the protein, which can be analyzed
via mass spectroscopy.]

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28
Q

How are Activity levels for enzymatic samples determined?

A

Activity levels for enzymatic samples are determined by following the process of a known reaction, often accompanied by a color change.

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29
Q

How is Protein concentration determined?

A

Protein concentration is also determined colorimetrically, either byUV spectroscopy or through a color change reaction.

BCA assay, Lowry reagent assay, and Bradford protein assay each
test for protein and have different advantages and disadvantages.

The Bradford protein assay, which uses a color change from browngreen to blue, is most common

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30
Q

How do cytoskeletal proteins differ from motor proteins?

A

Cytoskeletal proteins tend to be fibrous with repeating domains, while motor proteins tend to have ATPase activity and binding heads. Both types of protein function in cellular motility.

31
Q

True or False: Motor proteins are not enzymes.

A

False. An enzyme is a protein or RNA molecule with catalytic activity,
which motor proteins do have. Motor function is generally considered
nonenzymatic, but the ATPase functionality of motor proteins indicates
that these molecules do have catalytic activity

32
Q

What could permit a binding protein involved in sequestration to have a low affinity for its substrate and still have a high percentage of substrate bound?

A

If the binding protein is present in sufficiently high quantities relative to
the substrate, nearly all substrate will be bound despite a low affinity.

33
Q

Name the types of adhesion of a Cadherin, Integrin, and selectin:

A

Cadherin - Two cells of the same or similar type using calcium

Integrin - One cell to proteins in the extracellular matrix

Selectin - One cell to carbohydrates, usually on the surface of other cells

34
Q

When an antibody binds to its antigen, what are the three possible outcomes of this interaction?

A

Antigen–antibody interactions can result in neutralization of the
pathogen or toxin, opsonization (marking) of the antigen for
destruction, or creation of insoluble antigen–antibody complexes that
can be phagocytized and digested by macrophages (agglutination).

35
Q

What type of Ion Channel is active at all time?

A

Ungated channels are always open.

36
Q

How do transport kinetics differ from enzyme kinetics?

A

Transport kinetics display both Km and vmax values. They also can be
cooperative, like some binding proteins. However, transporters do not
have analogous Keq values for reactions because there is no catalysis.

37
Q

What separation methods can be used to isolate a protein on the basis of isoelectric
point?

A

Isoelectric focusing and ion-exchange chromatography both separate proteins based on charge; the charge of a protein in any given environment is determined by its isoelectric point (pI).

38
Q

What are the relative benefits of native PAGE compared to SDS-PAGE?

A

Native PAGE allows a complete protein to be recovered after analysis; it
also more accurately determines the relative globular size of proteins.
SDS-PAGE can be used to eliminate conflation from mass-to-charge
ratios.

39
Q

What are two potential drawbacks of affinity chromatography?

A

The protein of interest may not elute from the column because its
affinity is too high or it may be permanently bound to the free receptor
in the eluent.

40
Q

True or False: In size-exclusion chromatography, the largest molecules elute first

A

True. The small pores in size-exclusion chromatography trap smaller particles, retaining them in the column.

41
Q

Why are proteins analyzed after isolation?

A

Protein isolation is generally only the first step in an analysis. The protein identity must be confirmed by amino acid analysis or activity.
With unknown proteins, classification of their features is generally
desired.

42
Q

What factors would cause an activity assay to display lower activity than expected
after concentration determination?

A

Contamination of the sample with detergent or SDS could yield an
artificially increased protein level, leading to lower activity than expected (because the protein concentration was calculated as higher
than its actual value). Alternatively, the enzyme could have been
denatured during isolation and analysis.

43
Q

True or False: The Edman degradation proceeds from the carboxy (C-) terminus.

A

False. The Edman degradation proceeds from the amino (N-) terminus.

44
Q

What is the function of sodium dodecyl sulfate (SDS) in SDSPAGE?

A. SDS stabilizes the gel matrix, improving resolution during
electrophoresis.
B. SDS solubilizes proteins to give them uniformly negative
charges, so the separation is based purely on size.
C. SDS raises the pH of the gel, separating multiunit proteins into
individual subunits.
D. SDS solubilizes proteins to give them uniformly positive
charges, so separation is based purely on pH.

A

B.
Sodium dodecyl sulfate is a detergent and will digest proteins to form
micelles with uniform negative charges. Because the protein is sequestered
within the micelle, other factors such as charge of the protein and shape
have minimal roles during separation. In essence, the protein micelles can
be modeled as being spheres, dependent only on size.

45
Q

Which of the following is NOT involved in cell migration?
A. Dynein
B. Flagella
C. Actin
D. Centrioles

A

D
From the given choices, all of them are involved in cell movement with the
exception of (D). Centrioles are composed of microtubules, but are involved
in mitosis, not cell migration.

46
Q

Which of the following proteins is most likely to be found
extracellularly?
A. Tubulin
B. Myosin
C. Collagen
D. Actin

A

C
The most prevalent extracellular proteins are keratin, elastin, and collagen.
Tubulin and actin are the primary cytoskeletal proteins, while myosin is a
motor protein.

47
Q

Hormones are found in the body in very low concentrations, but
tend to have a strong effect. What type of receptor are hormones
most likely to act on?
I. Ligand-gated ion channels
II. Enzyme-linked receptors
III. G protein-coupled receptors
A. I only
B. III only
C. II and III only
D. I, II, and III

A

C
For a ligand present in low quantities to have a strong action, we expect it to
initiate a second messenger cascade system. Second messenger systems
amplify signals because enzymes can catalyze a reaction more than once
while they are active, and often activate other enzymes. Both enzyme-linked
receptors and G protein-coupled receptors use second messenger systems,
while ion channels do not.

48
Q

Which of the following is most likely to be found bound to a
protein in the body?
A. Sodium
B. Potassium
C. Chloride
D. Calcium

A

D
Ions that are not readily accessible in the cytoplasm or extracellular space
are likely to be bound to a binding protein. Classically, calcium and
magnesium are protein-bound. Without this background knowledge, the
question can still be answered. Sodium, (A), and potassium, (B), must exist
in their free states to participate in action potentials. Chloride, (C), is readily
excreted by the kidney, which would not be true if it were protein-bound.
Calcium must be sequestered in both the bloodstream and intracellularly
because calcium is used for muscle contraction, exocytosis (of
neurotransmitters and other signals), and many other cellular processes that
must be tightly regulated.

49
Q

Which of the following characteristics is NOT attributed to
antibodies?
A. Antibodies bind to more than one distinct antigen.
B. Antibodies label antigens for targeting by other immune cells.
C. Antibodies can cause agglutination by interaction with antigen.
D. Antibodies have two heavy chains and two light chains.

A

A
Antibodies are specific to a single antigen. Each B-cell produces a single type
of antibody with a constant region that is specific to the host and a variable
region that is specific to an antigen.

50
Q

Which ion channels are responsible for maintaining the resting
membrane potential?
A. Ungated channels
B. Voltage-gated channels
C. Ligand-gated channels
D. No ion channels are involved in maintenance of the resting
membrane potential.

A

A
The resting membrane potential is displayed by cells that are not actively
involved in signal transduction. Ungated or “leak” channels permit limited free flow of ions, while the sodium–potassium pump is also active and corrects for this leakage. Ligand-gated and voltage-gated channels are
involved in cell signaling and in the pacemaker potentials of certain cells, but cause deviation from—not maintenance of—the resting membrane
potential.

51
Q

Which of the following is NOT a component of all trimeric G
proteins?
A. Gα
B. Gβ
C. Gγ
D. Gi

A

D
All trimeric G proteins have α, β, and γ subunits—(A), (B), and (C), respectively. Gs , Gi
, and Gq are subtypes of the Gα subunit of the trimeric G
protein and differ depending on the G protein-coupled receptor’s function.

52
Q

Which of the following methods would be best to separate large
quantities of the following proteins? (Note: MM = molar mass)
Protein pI MM
Protein A. 6.5 28,000
Protein B 6.3 70,000
Protein C 6.6 200,000

A. Ion-exchange chromatography
B. Size-exclusion chromatography
C. Isoelectric focusing
D. Native PAGE

A

B
The proteins described in the question differ primarily in their molecular
weights. eir pI values are very close, so ion-exchange chromatography,
(A), is not a good choice. e question specifies a large quantity, which is
better processed through chromatography than through electrophoresis—
(C) and (D)—because the gel can only handle a small volume of protein.

53
Q

Which amino acids contribute most significantly to the pI of a
protein?
I. Lysine
II. Glycine
III. Arginine
A. I only
B. I and II only
C. I and III only
D. II and III only

A

C
The overall pI of a protein is determined by the relative number of acidic
and basic amino acids. e basic amino acids are arginine, lysine, and
histidine, and the acidic amino acids are aspartic acid and glutamic acid.
Glycine’s side chain is a hydrogen atom, so it will have the least contribution
of all the amino acids.

54
Q

How does the gel for isoelectric focusing differ from the gel for
traditional electrophoresis?

A. Isoelectric focusing uses a gel with much larger pore sizes to allow for complete migration.
B. Isoelectric focusing uses a gel with SDS added to encourage a uniform negative charge.
C. Isoelectric focusing uses a gel with a pH gradient that encourages a variable charge.
D. The gel is unchanged in isoelectric focusing; the protein mixture is treated before loading.

A

C
The gel in isoelectric focusing uses a pH gradient. When a protein is in a
region with a pH above its pI, it is negatively charged and moves toward the
anode. When it is in a pH region below its pI, it is positively charged and
moves toward the cathode. When the pH equals the pI, the migration of the
protein is halted

55
Q

Which protein properties allow UV spectroscopy to be used as a method of determining concentration?

A. Proteins have partially planar characteristics in peptide bonds.
B. Globular proteins cause scattering of light.
C. Proteins contain aromatic groups in certain amino acids.
D. All organic macromolecules can be assessed with UV
spectroscopy.

A

C
UV spectroscopy is best used with conjugated systems of double bonds.
While the double bond in the peptide bond does display resonance, this is
not adequate for UV absorption. However, aromatic systems are conjugated, and phenylalanine, tyrosine, and tryptophan all contain aromatic ring
structures

56
Q

A protein collected through affinity chromatography displays no activity even though it is found to have a high concentration using
the Bradford protein assay. What best explains these findings?
A. The Bradford reagent was prepared incorrectly.
B. The active site is occupied by free ligand.
C. The protein is bound to the column.
D. The protein does not catalyze the reaction of interest

A

B
Protein activity and concentration are generally correlated. Because we have
a high concentration of protein, we expect a high activity unless the protein
has been damaged or inactivated in some way. e protein could have been
inactivated by experimental conditions like detergents, heat, or pH; however,
these are not answer choices. Rather, we must consider how the
experimental procedure works. Protein elutes off of an affinity column by
binding free ligand. In this situation, the binding may not have been
reversed and thus the free ligand competes for the active site of the enzyme,
lowering its activity

57
Q

What property of protein-digesting enzymes allows for a
sequence to be determined without fully degrading the protein?
A. Selectivity
B. Sensitivity
C. Turnover
D. Inhibition

A

A
The selective cleavage of proteins by digestive enzymes allows fragments of different lengths with known amino acid endpoints to be created. By
cleaving the protein with several different enzymes, a basic outline of the
amino acid sequence can be created.

58
Q

What is blotting?

A

Blotting is a method of transferring fragments of protein, DNA, or RNA that have been separated via electrophoresis and applying them to a blotting membrane

You can then visualize the fragments with a colored stain

59
Q

In isoelectric focusing, the gel has a pH gradient and the proteins will migrate through the gel until they reach the pH that matches their _________

A

In isoelectric focusing, the gel has a pH gradient and the proteins will migrate through the gel until they reach the pH that matches their isoelectric point

At the pI, the protein has a neutral charge, so it will no longer be attracted to the anode or the cathode and it will stop migrating

60
Q

________ allow cells to adhere to carbohydrates on the surfaces of other cells and are most commonly used in the immune system

A

Selectins allow cells to adhere to carbohydrates on the surfaces of other cells and are most commonly used in the immune system

61
Q

________ have two membrane-spanning chains and permit cells to adhere to proteins in the extracellular matrix

A

Integrins have two membrane-spanning chains and permit cells to adhere to proteins in the extracellular matrix

62
Q

Enzyme-linked receptors participate in cell signaling through extracellular ligand binding and initiation of ___ ________ _________

A

Enzyme-linked receptors participate in cell signaling through extracellular ligand binding and initiation of 2nd messenger cascades

63
Q

______ channels open within a range of membrane potentials

A

Voltage-gated channels open within a range of membrane potentials

64
Q

In gel electrophoresis:

Small molecules move [fast or slow]

Large molecules move [fast or slow]

A

In gel electrophoresis:

Small molecules move fast

Large molecules move slow

Shorter molecules migrate more easily through the pores of the gel

65
Q

______ channels open in the presence of a specific binding substance, usually a hormone or neurotransmitter

A

Ligand-gated channels open in the presence of a specific binding substance, usually a hormone or neurotransmitter

66
Q

In SDS-PAGE, you can add an additional reducing agent called [_______] to reduce disulfide bonds. This further denatures the protein

A

In SDS-PAGE, you can add an additional reducing agent called 2-mercaptoethanol to reduce disulfide bonds. This further denatures the protein

67
Q

In gel electrophoresis:

[…] gel has large pores so it is used to separate nucleic acids

[…] gel has small pores so it is better for separating proteins

A

In gel electrophoresis:

Agarose gel has large pores so it is used to separate nucleic acids

Polyacrylamide gel has small pores so it is better for separating proteins

Nucleic acids are usually larger than proteins

68
Q

Agrose vs Polyacrylamide

A

Agrose:
Horizontal, Bigger gaps in Gel, seperates both large and small but better for larger molecules, CANNOT tell the difference between sizes of bands, Mostly DNA

Polyacrylamide:
Vertical, smaller gaps in gel, seperates both large and small but better for smaller molecules, CAN tell the difference between sizes of bands, Mostly DNA or proteins

69
Q

[…] are protein molecules that span across the cell membrane allowing the passage of ions from one side of the membrane to the other

A

Ion channels are protein molecules that span across the cell membrane allowing the passage of ions from one side of the membrane to the other

Examples of ion channels include:

Ungated channels (always open)
mechanically-gated channels
voltage-gated channels
ligand-gated channels

70
Q

________ blotting is used to detect a specific protein in a sample

A

Western blotting is used to detect a specific protein in a sample

71
Q

Gel electrophoresis is a technique commonly used in laboratories to separate charged molecules like DNA, RNA and proteins according to their […] and […]

A

Gel electrophoresis is a technique commonly used in laboratories to separate charged molecules like DNA, RNA and proteins according to their size and charge

Small molecules move fast

Large molecules move slow

72
Q

Native-PAGE is a polyacrylamide gel electrophoresis method for proteins using [denaturing or non-denaturing] conditions

A

Native-PAGE is a polyacrylamide gel electrophoresis method for proteins using non-denaturing conditions

It is run in the absence of sodium dodecyl sulfate (SDS), which would denature the proteins

73
Q

SDS-PAGE denatures proteins and separates them solely based on ____

A

SDS-PAGE denatures proteins and separates them solely based on mass

This allows you to estimate the protein’s molecular mass

74
Q

[…] detect molecules outside the cell then activate internal signal transduction pathways and, ultimately, cellular responses

A

G protein-coupled receptors detect molecules outside the cell then activate internal signal transduction pathways and, ultimately, cellular responses

The 1st messenger ligand initiates the 2nd messenger and the cascade response

75
Q

[…] denatures proteins and gives them a uniform negative charge

A

Sodium dodecyl sulfate (SDS) denatures proteins and gives them a uniform negative charge

76
Q

Ungated ion channels are [sometimes or always] open

A

Ungated ion channels are always open