Protein Structure- Function Flashcards

(36 cards)

1
Q

What is the 1. Monomer 2. Polymer 3. Covalent Bond of a protein?

A
  1. Amino Acid
  2. Polypeptide
  3. Peptide Bonds
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2
Q

What causes the difference properties in amino acids?

A

R Groups

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3
Q

What does the molecule of an amino acid consist of?

A

Amino group (N-H2) and Carboxyl group (OH-C=O)

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4
Q

How many different amino acids are there?

A

20

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5
Q

The composition of an amino acid determines the _____ of a protein.

A

Structure

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6
Q

What does it mean if an amino acid has a positive charge?

A

Basic

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7
Q

What does it mean if an amino acid has a negative charge?

A

Acidic

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8
Q

If a protein is hydrophilic, it is most likely what? (Polar or Nonpolar)

A

Polar

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9
Q

If a protein is hydrophobic, it is most likely what? (Polar or Nonpolar)

A

Nonpolar

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10
Q

What does a nonpolar amino acid consist of?

A

Hydrocarbon chains

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11
Q

What does a polar amino acid consist of?

A

OH or polar molecule from R group

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12
Q

What is another name for Cysteine (polar molecule)

A

Sulfidral

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13
Q

Amino acids linked by covalent bonds are called _______ _________.

A

Peptide bonds

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14
Q

Where does the bond form between amino acids?

A

The backbone between the amino and carboxyl group

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15
Q

Polypeptides consist of what?

A

Sequence of amino acids

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16
Q

A function protein consists of ____ polypeptides precisely twisted and folded in to a unique shape.

17
Q

The specific activities of proteins result from what?

A

Their 3D architecture

18
Q

What are the four levels of protein structure? Define each

A
  1. Primary- unique sequence of amino acids (polypeptide chain)
  2. Secondary- coils and folds in the polypeptide chain (consists of H-bonds)
  3. Tertiary- Determined by interactions among various side chains
  4. Quaternary- consists of multiple polypeptide chains
19
Q

What is Transthyretin?

A

A protein that in serum and CSF that transports the thyroid hormone thyroxine and vitamin A

20
Q

What is the primary structure of a protein?

A

Amino acid sequence dictated by covalent bonding through the backbone

21
Q

What is the secondary structure of a protein? Name the two types

A

Twists and folds of structure.

  1. Alpha helix
  2. Beta pleated sheet
22
Q

What kind of bonding is found in secondary structures?

23
Q

How often are H-bonds in alpha helices?

A

Every 4th peptide bond

24
Q

What is the most common type of secondary structure to across membranes?

25
What are the two types of beta sheets?
Parallel ->,-> | Anti-parallel ->,
26
How often are H-bonds in beta sheets?
Typically 3-10 amino acids
27
How many strands are needed to form a beta sheet?
2 or more
28
What determines the tertiary structure?
The primary and secondary structures
29
What does a tertiary structure depend on ?
The R group and how they interact
30
Which R groups have ionic bonds?
Acidic/basic
31
What R groups are hydrophobic?
Nonpolar R groups
32
What is the strongest bond formed between amino acids?
Disulfide Bridge
33
What is a quaternary structure?
More than one polypeptide subunit
34
What impacts protein structure? (4)
1. Temperature 2. Solvent 3. pH 4. Salt concentration
35
What is denaturation?
The unraveling of proteins in the tertiary and secondary structures
36
What is a disease linked to a change in primary structure?
Sickle Cell disease