Chapter 19 Flashcards

(45 cards)

1
Q

Explain Proteins.

A

Proteins…
- in the body are polymers from 20 different amino acids
- form structural components such as cartilage, muscle, hair, and nails
- transport oxygen into the blood

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2
Q

What are Amino Acids?

A

Amino acids are molecular building blocks of proteins. They have a central atom called the alpha carbon.

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3
Q

What is the alpha carbon bonded to within amino acids?

A

The alpha carbon is bonded to…
- two functional groups: an ammonium group and a carboxylate group
- a hydrogen atom and a R group or side chain in addition to the carboxylate and ammonium group.

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4
Q

What are the classifications of Amino Acids?

A

Hydrophobic (water fearing)
- nonpolar neutral

Hydrophilic (water loving)
- polar neutral

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5
Q

T/F Our bodies can only metabolize the “L” form of amino acids.

A

True

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6
Q

How do you identify a Nonpolar Amino Acid?

A

An amino acid is nonpolar when the R group is H, alkyl, or aromatic.

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7
Q

How do you identify a Polar Amino Acid?

A

An amino acid is polar when the R group is an alcohol, thiol, or amide.

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8
Q

How do you identify a Polar Acidic Amino Acid?

A

An amino acid is polar acidic when the R group is a carboxylate group (when its negative).

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9
Q

How do you identify a Polar Basic Amino Acid?

A

An amino acid is polar basic when the R group is a ammonium group (when its postive).

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10
Q

Classify this Amino Acid.

A

Nonpolar

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11
Q

Classify this Amino Acid.

A

Nonpolar

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12
Q

Classify this Amino Acid.

A

Nonpolar

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13
Q

Classify this Amino Acid.

A

Nonpolar

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14
Q

Classify this Amino Acid.

A

Nonpolar

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15
Q

Classify this Amino Acid.

A

Nonpolar

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16
Q

Classify this Amino Acid.

A

Nonpolar

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17
Q

Classify this Amino Acid.

A

Nonpolar

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18
Q

Classify this Amino Acid.

A

Nonpolar

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19
Q

Classify this Amino Acid.

20
Q

Classify this Amino Acid.

21
Q

Classify this Amino Acid.

22
Q

Classify this Amino Acid.

23
Q

Classify this Amino Acid.

24
Q

Classify this Amino Acid.

25
Classify this Amino Acid.
Polar Acidic
26
Classify this Amino Acid.
Polar Acidic
27
Classify this Amino Acid.
Polar Basic
28
Classify this Amino Acid.
Polar Basic
29
Classify this Amino Acid.
Polar Basic
30
What are Peptides?
Shorter chains of amino acids are called peptides - Longer chains are called polypeptides - The N terminal amino acid is written on the left and the C terminal is written on the right.
31
What is a Peptide Bond?
Peptide bonds are amide bonds between the alpha carbon group of one amino acid and the carboxylic acid group of another amino acid.
32
Explain how to draw Peptides.
1. Draw the structure for each amino acid peptide 2. Remove the O- atom from the carboxylate group 3. Remove two H+ atoms from the ammonium group 4. Use peptide bonds to connect the amino acids
33
Explain Primary Structure of Proteins.
- a sequence of amino acids in a protein - slight changes in the sequence can greatly affect protein function - sickle cell anemia is caused by substitution of a single amino acid.
34
Explain Insulin.
Insulin was the first protein to have its primary structure determined. It has a primary structure of two polypeptide chains linked by disulfide bonds.
35
Explain Secondary Structure of Proteins.
- These structures are maintained by numerous hydrogen bonds between the C=O and NH groups of the peptide bonds. - Two common types include alpha helices and beta pleated sheets. - The formation of many hydrogen bonds along the polypeptide chain gives the helical shape.
36
Explain a Triple Helix.
- Three polypeptide chains woven together - Hydrogen bonds hold the chains together giving the polypeptide the added strength collagen, connective tissue, and tendons.
37
Explain Tertiary Structure of Proteins.
Its a three dimensional shape formed by the interactions of amino acids readiness in different parts of the chain. There are 5 stabilizing interactions: 1. Hydrophobic Interactions 2. Hydrophilic Interactions 3. Salt Bridges 4. Hydrogen Bonds 5. Disulfide Bonds
38
Explain Hydrophobic Interactions.
Occur between two amino acids that have nonpolar R groups, forming a nonpolar center at the interior of the protein.
39
Explain Hydrophilic Interactions.
Occur between the external aqueous environment and the R groups of the polar amino acid residues that are pulled to the outer surface of most proteins.
40
Explain Salt Bridges.
Are ionic attractions between ionized R groups of polar basic and polar acidic amino acids.
41
Explain Hydrogen Bonds.
Form between the H of a polar R group and the O and N of another polar amino acid.
42
Explain Disulfide Bonds.
Are covalent bonds that form between SH groups of cysteine residues in a polypeptide chain.
43
Explain Quaternary Structure of Proteins.
- Biologically active proteins with two or more polypeptide chains or subunits. - Hemoglobin (a globular protein that transports oxygen in blood) consist of four polypeptide chains: two alpha and two beta chains.
44
What is Denaturation of a Protein?
Denaturation of a protein occurs when the interaction that stabilizes secondary, tertiary, or quaternary structures are disrupted. - it destroy the shape and renders the protein biological inactive - it does not alter the primary structure of the protein
45
How does Denaturation of a Protein occur?
- Increasing temperature - Making the pH very acidic or basic - Adding a certain organic compound - Adding a heavy metal ion - Adding mechanical agitation