Nonenzymatic Protein Function and Protein Analysis Flashcards

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1
Q

Structural Proteins definition and examples

A

Compose the cytoskeleton, anchoring proteins, and
much of the extracellular matrix. The most common
structural proteins are collagen, elastin, keratin, actin,
and tubulin. They are generally fibrous in nature.

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2
Q

Motor Proteins and examples

A

Have one or more heads capable of force generation
through a conformational change. They have catalytic
activity, acting as ATPases to power mvmt. Common
applications include muscle contraction, vesicle mvmt
within cells, and cell motility.

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3
Q

Give Examples of Motor Proteins

A

myosin, kinesin, and dynein.

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4
Q

Binding Proteins

A

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

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5
Q

G Protein-Coupled
Receptors

A

GPCR has a membrane-bound protein called the GProtein
(a, b, y subunits). The 1st messenger ligand
initiates the 2nd messenger and the cascade response

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6
Q

Cell adhesion molecules

A

Allow cells to bind to other cells or surfaces.

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7
Q

Cell adhesion molecules: Cadherins

A

Calcium dependent glycoproteins that
hold similar cells together.

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8
Q

Cell Adhesion
Molecules (CAM): Integrins

A

Have two membrane-spanning chains and
permit cells to adhere to proteins in the extracellular
matrix.

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9
Q

Cell Adhesion
Molecules (CAM): Selectins

A

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

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10
Q

Antibodies

A

Immunoglobulins, Ig. Used by the immune system to
target a specific antigen, which may be a protein on
the surface of a pathogen or a toxin. The variable
region is responsible for antigen binding.

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11
Q

Electrophoresis

A

Uses a gel matrix to observe the migration of proteins in
responses to an electric field

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12
Q

Native PAGE:

A

: Maintains the protein’s shape, but results are difficult to
compare because the mass / charge ratio differs for
each protein.

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13
Q

SDS-PAGE

A

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

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14
Q

Isoelectric
Focusing:

A

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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15
Q

Chromatography

A

Separates protein mixtures on the basis of their affinity
for a stationary phase or a mobile phase

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16
Q

Column
Chromatography

A

Uses beads of a polar compound (stationary phase) with
a nonpolar solvent (mobile phase).

17
Q

Ion-Exchange
Chromatography

A

Uses a charged column and a variably saline eluent.

18
Q

Size-Exclusion
Chromatography

A

Relies on porous beads. Larger molecules elute first
because they are not trapped in the small pores.

19
Q

Affinity
Chromatography

A

Uses a bound receptor or ligand and an eluent with free
ligand or a receptor for the protein of interest.

20
Q

Ungated ion Channels

A

Always open

21
Q

Voltage-Gated Channels

A

Open within a range of
membrane potentials.

22
Q

Ligand-Gated Channels:

A

Open in the presence of a
specific binding substance, usually a hormone or
neurotransmitter.

23
Q

Enzyme-Linked
Receptors

A

Participate in cell signaling through extracellular ligand
binding and initiation of 2nd messenger cascades

24
Q

How is the protein structure determined?

A

Primarily determined through x-ray crystallography
after the protein is isolated, although NMR can also be
used.

25
Q

How is an amino acid sequence determined?

A

Edman degradation

26
Q

How is protein concentration determined?

A

Determined colorimetrically, either by UV
spectroscopy or through a color change reaction.
Bradford Assay, BCA Assay, and Lowry Reagent Assay
each test for protein and have different advantages
and disadvantages. The Bradford Protein Assay is most
common. It uses a color change from brown-green –>
blue.

27
Q

How to determine absorbance of a protein?

A

Beer-lambert law: Absorbance = eCl

e= extinction coefficient C=concentration

l = path length in cm