biochemistry chapter 3

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42 Terms

1
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What do structural proteins compose?

Cytoskeleton, Anchoring proteins, Extracellular matrix

2
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Name two common structural proteins.

Collagen, Elastin, Keratin, Actin, Tubulin

3
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How are motor proteins characterized?

By having one or more heads capable of generating force through conformational change.

4
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List one application of motor proteins.

Muscle contraction, Vesicle movement within cells, Cell motility

5
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Give examples of motor proteins.

Myosin, Kinesin, Dynein

6
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What is the role of binding proteins?

To bind a specific substrate, sequestering it or holding its concentration steady.

7
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What do cell adhesion molecules (CAM) do?

Allow cells to bind to other cells or surfaces.

8
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What are cadherins?

Calcium-dependent glycoproteins that hold similar cells together.

9
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Describe integrins.

They have two membrane-spanning chains and allow cells to adhere to proteins in the extracellular matrix.

10
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What role do selectins play in the body?

Allow cells to adhere to carbohydrates on the surfaces of other cells, notably in the immune system.

11
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What are antibodies (immunoglobulins) used for?

To target a specific antigen, such as a protein on a pathogen or a toxin.

12
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Describe the structure of an antibody.

Made of two identical heavy chains and two light chains, held by disulfide linkages.

13
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What are the three types of ion channels?

Ungated, Voltage-gated, Ligand-gated

14
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How do ungated channels function?

They are always open.

15
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What triggers voltage-gated channels to open?

Changes in membrane potential.

16
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What is the function of ligand-gated channels?

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

17
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What role do enzyme-linked receptors play in cell signaling?

They bind extracellular ligands and initiate second messenger cascades.

18
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What are G protein-coupled receptors associated with?

A trimeric G protein that initiates second messenger systems.

19
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What happens to GDP when a ligand binds to a G protein?

GDP is replaced with GTP, activating the G protein.

20
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What does the activated α subunit do?

It alters the activity of adenylate cyclase or phospholipase C.

21
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What occurs when GTP is dephosphorylated?

The α subunit rebinds to the β and γ subunits.

22
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What technique does electrophoresis use?

A gel matrix to observe the migration of proteins in an electric field.

23
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What is the purpose of native PAGE?

It maintains protein shape but results are hard to compare due to varying mass-to-charge ratios.

24
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What does SDS-PAGE do to proteins?

Denatures them and masks the native charge for accurate size comparison.

25
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How does isoelectric focusing work?

It separates proteins by pI; proteins migrate until pH = pI.

26
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What is the function of chromatography in protein analysis?

Separates protein mixtures based on affinity to stationary or mobile phases.

27
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What is used in column chromatography?

Beads of a polar compound with a nonpolar solvent.

28
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What characterizes ion-exchange chromatography?

A charged column and a variably saline eluent.

29
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What does size-exclusion chromatography rely on?

Porous beads; larger molecules elute first.

30
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What is utilized in affinity chromatography?

A bound receptor or ligand and an eluent with free ligand or receptor.

31
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How can amino acid composition be determined?

By simple hydrolysis.

32
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What process is used for amino acid sequencing?

Sequential degradation like Edman degradation.

33
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How is enzyme activity determined?

By following the process of a known reaction, often with a color change.

34
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How can protein concentration be measured?

Colorimetrically, using either UV spectroscopy or color change reactions.

35
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What color change occurs in the Bradford protein assay?

From brown-green to blue.

36
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What method primarily determines protein structure?

X-ray crystallography

37
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Which technique can also be used alongside X-ray crystallography?

NMR (Nuclear Magnetic Resonance)

38
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How is amino acid composition determined?

By simple hydrolysis

39
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What process is required for amino acid sequencing?

Sequential degradation (e.g., Edman degradation)

40
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How are activity levels of enzymatic samples determined?

By following a known reaction which often shows a color change

41
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What are the methods to determine protein concentration?

Colorimetrically, using UV spectroscopy or color change reactions

42
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What is the common method for protein concentration analysis?

The Bradford protein assay