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BMS 300- Unit 1 > Lecture 3- Lipid Bilayer/Proteins > Flashcards

Lecture 3- Lipid Bilayer/Proteins Flashcards

1
Q

What are the 3 key features of a phospholipid structure?

A
  1. Modified triglyceride
  2. R group (choline, serine, or ethanol-amine)
  3. Amphipathic properties
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2
Q

What two features make up phospholipids?

Which are hydrophobic/hydrophilic?

A

Head- hydrophilic
Tail- hydrophobic

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3
Q

Which is more stable, micelle or liposome?

A

Liposome

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4
Q

What is a single-layer lipid sphere called? What type of stability does this structure have?

A

Micelle/unstable

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5
Q

What is a lipid-bilayer sphere called? What type of stability does this structure have?

A

Liposome/stable

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6
Q

How do phospholipid heads compare to cell shape in a planar lipid bilayer?

A

Cell is much larger than phospholipid heads, so many phospholipid heads are required in a curvature style to match the cell size

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7
Q

What is the lipid bilayer punctured with?

A

Proteins

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8
Q

What are three integral membrane protein functions?

A
  1. Cellular communication
  2. Maintain ion concentrations
  3. Protein stability
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9
Q

What is the pathway of protein production?

A

DNA————->RNA———–>Protein
transcription translation

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10
Q

What are primary proteins made of?

A

Sequences of amino acids

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11
Q

How are secondary proteins made?

A

Local folding of the polypeptide chain into helices and sheets

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12
Q

What are examples of secondary protein structures?

A

Helices and sheets

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13
Q

How are tertiary protein structures made?

A

3D folding pattern of protein due to side chain interactions

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14
Q

True or false? Both alpha helices and beta sheets are used in tertiary protein structures.

A

True

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15
Q

What are quaternary protein structures made of?

A

Protein that consists of more than one amino acid chain

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16
Q

What are proteins constructed from?

A

Amino acids

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17
Q

What do all amino acids contain? (3 things)

A

Carboxyl group and an amino group linked by a carbon. R-group attaches to carbon

18
Q

What changes to produce various amino acids?

A

The R-group

19
Q

True or false? Some R-group are hydrophobic while some are hydrophilic

A

True

20
Q

How many amino acids are there?

A

20

21
Q

How are amino acids linked to one another?

A

Peptide bond

22
Q

How does a peptide bond form?

A

Carbon on carboxyl group forms covalent bond with nitrogen in the amine group in adjacent amino acid

23
Q

Are alpha helices or beta sheets more common?

A

Alpha helices

24
Q

What is the alpha helices bonding sequence?

A

i +4 H bonding
Each peptide bond C-O is hydrogen bonded to the peptide bond N-H, four amino acid residues ahead of it

25
Q

Which way do side chains face from the helix axis in alpha helices?

A

Outward

26
Q

True or false? Beta sheets are more extended than alpha helices?

A

True

27
Q

How do polypeptides lay in beta sheets?

A

Side by side

28
Q

What type of interactions mainly form tertiary structures?

A

Hydrophobic interactions

29
Q

In the tertiary structures what do non-polar groups form?

A

Hydrophobic core

30
Q

In the tertiary structures what do polar groups form?

A

Hydrophilic shell

31
Q

What are quaternary structures defined by?

A

Interactions between different polypeptides

32
Q

What are 5 examples of proteins?

A
  1. Receptors
  2. Hormones
  3. Enzymes
  4. Transport proteins (protein channels)
  5. Antibodies
33
Q

What five things determine protein shape?

A
  1. Type of amino acids
  2. Order of amino acids
  3. # of amino acids
  4. Bonds between amino acids
  5. Environmental factors (temperature/pH)
34
Q

What are prions?

A

Bad proteins
Abnormal, pathogenic agents that are transmissible and are able to induce abnormal folding of specific normal cellular proteins called prion proteins that are found most abundantly in the brain

35
Q

What are examples of animal prions?

A

Scrapie, bovine spongiform encephalopathy

SBSE

36
Q

What are examples of human prions?

A

Creutzfeldt-Jakob Disease (CJB), Kuru

37
Q

What three things determine protein structure?

A
  1. Amino acid sequence
  2. Bonds
  3. Environment
38
Q

Potassium ions can pass through a biological membrane by moving

-Directly across the lipid bilayer
-Through transmembrane lipid channels
-Through transmembrane protein channels lined with hydrophobic amino acids
-Through transmembrane protein channels lined with hydrophilic amino acids
-Through transmembrane protein channels lined with uncharged amino acids

A

Through transmembrane protein channels lined with hydrophilic amino acids

39
Q

In the lipid mosaic model of the membrane, _________ normally form the ion channels.

-Amphipathic phosphate head groups
-Alpha helices
-Beta sheets
-Phospholipids
-Triglycerides

A

Alpha helices

Alpha helices are proteins embedded in the lipid bilayer. Their R-groups are hydrophobic and interact with hydrophobic phospholipid tails.

40
Q

Hydrogen bonding between the carbonyl oxygen of one amino acid and the hydrogen on the amine of the nearby amino acid is responsible for the ____ structure in proteins.

Primary
Secondary
Alpha helical
More than one answer is correct

A

More than one answer is correct

Alpha helices are secondary proteins

41
Q

The charge and orientation of R-groups on amino acids are important in determining all of the following except:

-Its 3D shape
-Its tertiary structure
-The type of ligand or substrate it will bind
-The type of ion that will pass through its transmembrane channel
-The secondary structure within the protein

A

The secondary structure within the protein

Hydrogen bonds and peptide bonds determine secondary structure. Not R-groups

42
Q

Aquaporins are proteins that span the phospholipid bilayer of cells.
What protein structure is most likely associated with the transmembrane portion of the aquaporin channels?

-An amino acid chain with hydrogen bonds formed between the peptide bonds
-A sequence of amino acids joined by peptide bonds
-Multiple protein subunits joined together by non-covalent forces
-An amino acid chain with hydrogen bonds between R groups

A

An amino acid chain with hydrogen bonds formed between the peptide bonds

(Alpha helices are embedded in aquaporin channels)

BMS 300- Unit 1 (12 decks)

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