Week 4 Flashcards

(57 cards)

1
Q

_____________ the building blocks of proteins.

A

Amino Acids.

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2
Q

Amino acids contain ____________ and _____________ functional groups.

A

Amine and carboxylic acid.

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3
Q

In nature the ___________ enantiomer of the amino acid is commonly found.

A

L

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4
Q

______________ is a molecule that possesses both a positive and negative charge.

A

Zwitterion

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5
Q

_____________ side chains are non polar and incapable of hydrogen bonding.

A

Hydrophobic

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6
Q

_____________charged amino acids contain a carboxyl group and are commonly ____________ at physiological pH.

A

Negatively, deprotonated.

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7
Q

______________ charged amino acids include lysine, arginine, and histidine.

A

Positively

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8
Q

Amino acids serve a variety of roles in biochemistry including:

A
  1. Lipid metabolism
  2. Amino acid catabolism
  3. Neurotransmission
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9
Q

Why is proline the least flexible amino acid?

A

Its side chain is bonded to its amino group.

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10
Q

_________ is the linkage between two amino acids.

A

Peptide bond.

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11
Q

A peptide bond is an _________ linkage between the __________ group of amino acid and the ___________ group of the next.

A

Amide,carboxyl, amino.

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12
Q

A _____________ molecule is removed in order for an amide bond to form.

A

Water.

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13
Q

_____________ are nonprotein groups required for protein binding or activity.

A

Cofactor.

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14
Q

Cofactors can be divided into two common categories:

A

Minerals(metal and ions) and vitamins (small organic groups.

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15
Q

___________ are enzymes that catalyze phosphorylation reaction.

A

Kinases.

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16
Q

____________ is typically the source of phosphate.

A

ATP.

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17
Q

______________ can change the activity of an enzyme and is thought to act as switch in the cell.

A

Phosphorylation.

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18
Q

A peptide bond is normally an amide but also is capable of mildly acting as what?

A

An oxime.

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19
Q

What are the 4 levels of protein structure?

A
  1. Primary
  2. Secondary
  3. Tertiary
    4.Quaternary
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20
Q

The _____________ structure is the linear arrangement of amino acids.

A

Primary.

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21
Q

The ____________ structure is held together by hydrogen bonding.

A

Secondary.

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22
Q

The secondary structure consists of two major structural elements:

A

Alpha helix and Beta sheet

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23
Q

____________ is the most common structure observed in proteins.

24
Q

_____________ can be parallel or anti-parallel.

25
In anti-parallel beta sheets the hydrogen bonds are __________.
Linear.
26
In parallel beta sheets the hydrogen bonds are __________.
Horizontal.
27
___________ and ____________ limit the flexibility of the peptide chain.
Hairpin and Loops.
28
____________ structure gives the overall shape of the protein.
Tertiary.
29
___________ are combinations of secondary structure.
Motifs
30
___________ pieces of a protein that retain their structure in the absence of the rest of the protein.
Domains.
31
What are the bonding forces involved in stabilizing tertiary structure?
1. Hydrogen bonding 2. London dispersion forces 3. Dipole-dipole interactions 4. Salt bridges 5. Cation interactions 6. Disulfide bonds
32
___________ describes the phenomenon in which hydrophobic groups cluster together.
Hydrophobic effect.
33
____________ structure is a complex structure that incorporates multiple subunits or different proteins.
Quaternary
34
Which amino acid can donate the most hydrogen bonds?
Arginine.
35
__________ a protein that acts as a pore in the membrane, it selectively allows water to pass in and out of the cell.
Aquaporin.
36
Aquaporin is a ___________ protein that consists of 6 transmembrane alpha helices.
Transmembrane.
37
__________ is an enzyme that cleaves dietary into peptides.
Chymotrypsin.
38
Chymotrypsin is produced by the _________ and secreted into the ____________.
Pancreas, Intestinal lumen.
39
Chymotrypsin is composed of __________ beta barrels and ____________ short alpha helix.
Two and one.
40
__________ is a fibrous protein mostly concentrated in muscle and connective tissue.
Collagen.
41
Collagen is composed of a triple helix that contains __________, _____________, and ______________.
Glycine, proline, and hydroxyproline.
42
____________ is a globular, tetrameric protein found in red blood cells.
Hemoglobin.
43
Hemoglobin uses heme as a ___________ for each subunit.
Cofactor.
44
Hemoglobin is a ____________ protein.
Transport.
45
Collagen is a __________ protein.
Structural.
46
_____________ are molecules of the immune system that recognize and bind to antigens.
Immunoglobulins.
47
Immunoglobulins are __________ proteins.
Binding.
48
____________ is a protein hormone produced by pancreatic beta cells.
Insulin.
49
Interrupted or impaired insulin signaling can result in __________.
Diabetes.
50
____________ diabetes is a failure to produce insulin.
Type I
51
___________ diabetes insulin is not received.
Type II
52
__________ acts as molecular motor in which energy is used to elicit a muscle contraction and transport vesicles in the cell.
Myosin.
53
Myosin contains___________ chains and ____________ chains.
Heavy and light.
54
_____________ chain interacts with the cytoskeletal protein_________.
Heavy, actin.
55
__________ chain plays a role in binding Ca+2.
Light chains.
56
Myosin is a _____________ protein.
Molecular motor.
57
How many subunits does hemoglobin have?
4