Chapter 3: Nonenzymatic Protein Function and Protein Analysis Flashcards

(39 cards)

1
Q

____________ has a characteristic trihelical fiber (three left-handed helices woven together to form a secondary right-handed helix) and makes up most of the extracellular matrix of connective tissue.

A

Collagen

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2
Q

___________ is another important component of the extracellular matrix of connective tissue.

A

Elastin

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3
Q

____________ are intermediate filament proteins found in epithelial cells.

A

Keratins

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4
Q

__________ is a protein that makes up microfilaments and the thin filaments in myofibrils. It is the most abundant proteins in eukaryotic cells. It has a positive side and negative side.

A

Actin

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5
Q

__________ is the protein that makes up microtubules. It has polarity.

A

Tubule

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6
Q

_____________ motor proteins play key roles in aligning chromosomes during metaphase and depolymerizing microtubules during anaphase of mitosis.

A

Kinesins

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7
Q

___________ motor proteins are involved in the sliding movement oof cilia and flagella.

A

Dyneins

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8
Q

___________________ (_________) are proteins found on the surface of most cells and aid in binding the cell to the extracellular matrix or other cells.

A

Cell adhesion molecules (CAMs)

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9
Q

______________ are a group of glycoproteins that meditate calcium-dependent cell adhesion.

A

Cadherins

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10
Q

___________ are a group of proteins that all have two membrane-spanning chains called alpha and beta. They play a role in host immune defense.

A

Integrins

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11
Q

___________ are unique because they bind to carbohydrate molecules that project from other cell surfaces. They are expressed on WBCs and the endothelial cells that line blood vessels.

A

Selectins

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12
Q

_______________, a type of passive transport, is a diffusion of molecules down a concentration gradient through a pore in the membrane created by this transmembrane protein.

A

Facilitated diffusion

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13
Q

______________ is used for molecules that are impermeable to the membrane (large, polar, or charged).

A

Facilitated diffusion

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14
Q

______________ have no gates and are therefore unregulated.

A

Ungated channels

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15
Q

In _________________, the gate is regulated by the membrane potential change near the channel.

A

Voltage-gated channels

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16
Q

For __________________, the binding of a specific substance or ligand to the channel causes it to open or close.

A

Ligand-gated channels

17
Q

The ________________ have 3 primary protein domains: a membrane-spanning domain, a ligand binding domain, and a catalytic domain.

A

Enzyme-linked receptors

18
Q

Three main types of heterotrimeric G proteins:
____________
____________
____________

19
Q

________ stimulates adenylate cyclase, which increases levels of cAMP in the cell.

20
Q

________ inhibits adenylate cyclase, which decreases levels of cAMP in the cell.

21
Q

_______ activates phospholipase C, which cleaves a phospholipid from the membrane to form PIP2.

22
Q

Proteins and other biomolecules are isolated from body tissues or cell cultures by cell lysis and ________________ - crushing, grinding, or blending the tissue of interest into an evenly mixed solution.

A

Homogenization

23
Q

________________ can isolate proteins from much smaller molecules before other isolation techniques must be employed.

A

Centrifugation

24
Q

________________ works by subjecting compounds to an electric field, which moves proteins according too their net charge and size.

A

Electrophoresis

25
______________________ (_______) is a method for analyzing proteins in their native states. Unfortunately, it is limited by the varying mass-to-charge and mass-to-size ratios of cellular proteins because multiple different proteins may experience the same level of migration.
Polyacrylamide gel electrophoresis (PAGE)
26
___________________ is most useful to compare the molecular size or the charge of proteins known to be similar in size.
Polyacrylamide gel electrophoresis (PAGE)
27
___________________ (_______) - polyacrylamide gel electrophoresis is useful tool because it separates proteins on the basis of relative molecular mass alone.
Sodium dodecyl sulfate (SDS)
28
______________ exploits the acidic and basic properties of amino acids by separating on the basis of isoelectric point (pI).
Isoelectric focusing
29
Proteins that are positively charged will begin migrating toward the cathode and proteins that are negatively charged will begin migrating toward the anode. As the protein reaches the portion of gel where the pH is equal to the protein's pI, the protein takes on a neutral charge and will stop moving. This is the description of ________________.
Isoelectric focusing
30
Anode in isoelectric focusing: A+ Anode has __________ (H+ rich) gel and a (_____) charge.
Anode has acidic (H+ rich) gel and a (+) charge
31
________________ is another tool that uses physical and chemical properties to separate and identify compounds from a complex mixture.
Chromatography
32
Before _____________________ analysis, the protein must be isolated and crystallized.
X-ray crystallography
33
_________________ measures electron density on an extremely high-resolution scale and can also be used for nucleic acids.
Crystallography
34
The small dots in the diffraction pattern from ____________________ can then be interpreted to determine the protein's structure.
X-ray crystallography
35
Small proteins are best analyzed with the _________________, which uses cleavage to sequence proteins of up to 50 to 70 amino acids.
Edman degradation
36
Protein concentration is determined almost exclusively through ________________.
Spectroscopy
37
Because proteins contain aromatic side chains, they can be analyzed with ________________ without any treatment; however this type of analysis is particularly sensitive to sample contaminants.
UV spectroscopy
38
Proteins cause colorimetric changes with specific reactions, particularly the _________________ (______) assay, _________________ assay, and __________________ assay.
- Bicinchoninic assay (BCA) assay - Lowry reagent assay - Bradford protein assay
39
The _________________ mixes a protein in solution with Coomassie Brilliant Blue dye. The due is protonated and gives up protons upon binding to amino acid groups, turning blue in the process.
Bradford protein assay