Ch 3: Nonenzymatic Protein Function and Protein Analysis Flashcards

1
Q

Cell Adhesion Molecules (CAMs)

A

allow cells to bind to other cells or surfaces

cadherins, integrins, selectins

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2
Q

compose the cytoskeleton, anchoring proteins, and much of the extracellular matrix

A

structural proteins

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3
Q

most common structural proteins are

A

collagen, elastin, keratin, actin, and tubulin

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4
Q

motor proteins

A

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

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

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5
Q

myosin, kinesin, and dynein are all examples of

A

motor proteins

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6
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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7
Q

cadherins

A

CAM that are calcium-dependent glycoproteins that hold similar cells together

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8
Q

integrins

A

CAM 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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9
Q

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 (of immunoglobins, Ig)

A

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

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11
Q

Immunglobins contain

A

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

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12
Q

2 identical heavy chains and 2 identical light chains form an ____ and are held together by

A

antibody

disulfide bonds and noncovalent interactions

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13
Q

Ion channels

3 main types are

A

cen be used for regulating ion flow into or out of a cell

ungated channels, voltage-gated channels, ligand-gated channels

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14
Q

ungated channels

A

are always open

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15
Q

voltage-gated channels

A

open within a range of membrane potentials

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16
Q

ligand-gated channels

A

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

17
Q

Enzyme-linked receptors

A

participate in cell signaling through extracellular ligand binding and initiation of second messenger cascades

18
Q

G protein-coupled receptors

A

membrane-bound protein associated with trimetric G protein;

19
Q

G protein-coupled receptors also initiate second messenger systems

A

ligand binding engages the G protein,

GDP is replaced with GTP; the alpha subunit dissociates from the beta and gamma subunits,

the activated alpha subunit alters the activity of adenylate cyclase or phospholipase C

GTP is dephosphorylated to GDP; then alpha subunit rebinds to the beta and gamma subunits

20
Q

Electrophoresis

A

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

21
Q

Native PAGE (electrophoresis)

A

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

22
Q

SDS-PAGE (electrophoresis)

A

denatures the proteins and masks the native charge so that the comparison of size is more accurate, but the functional protein can not be recaptured from the gel

23
Q

Isoelectric focusing (electrophoresis)

A

seperates 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

24
Q

Chromatography

A

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

25
Q

Column Chromatography

A

uses beads of a polar compound, like silica or alumina (stationary phase) with a nonpolar solvent (mobile phase)

26
Q

Ion-Exchange Chromatography

A

uses a charged column and a variably saline eluent

27
Q

Size-exclusion Chromatography

A

relies on porous beads; larger molecules elute first because they are not trapped in the small pores

28
Q

Affinity Chromatography

A

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

29
Q

protein structure is primarily determined through _____ after the protein is isolated, though ___ can also be used

A

xray crystallography

NMR

30
Q

amino acid composition can be determined by ____ but amino acid sequencing required sequential degradation, such as ___

A

simple hydrolysis

Edman degradation

31
Q

activity levels for enzymatic samples are determined by following the process of a known reaction, often accompanied by a ___

A

color change

32
Q

protein concentration is also determined by ____ , either by ____ or through a color change reaction

A

colorimetrically

UV spectroscopy

33
Q

BCA assay, Lowry reagent assay, and Bradford protein assay each test for

A

protein, and have different advantages and disadvantages

34
Q

Bradford Protein assay is the most common and

A

uses a color change from brown-green to blue