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Biochemistry > Week 4 > Flashcards

Week 4 Flashcards

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.

A

Alpha helix

24
Q

_____________ can be parallel or anti-parallel.

A

Beta sheet.

25
Q

In anti-parallel beta sheets the hydrogen bonds are __________.

A

Linear.

26
Q

In parallel beta sheets the hydrogen bonds are __________.

A

Horizontal.

27
Q

___________ and ____________ limit the flexibility of the peptide chain.

A

Hairpin and Loops.

28
Q

____________ structure gives the overall shape of the protein.

A

Tertiary.

29
Q

___________ are combinations of secondary structure.

A

Motifs

30
Q

___________ pieces of a protein that retain their structure in the absence of the rest of the protein.

A

Domains.

31
Q

What are the bonding forces involved in stabilizing tertiary structure?

A
  1. Hydrogen bonding
  2. London dispersion forces
  3. Dipole-dipole interactions
  4. Salt bridges
  5. Cation interactions
  6. Disulfide bonds
32
Q

___________ describes the phenomenon in which hydrophobic groups cluster together.

A

Hydrophobic effect.

33
Q

____________ structure is a complex structure that incorporates multiple subunits or different proteins.

A

Quaternary

34
Q

Which amino acid can donate the most hydrogen bonds?

A

Arginine.

35
Q

__________ a protein that acts as a pore in the membrane, it selectively allows water to pass in and out of the cell.

A

Aquaporin.

36
Q

Aquaporin is a ___________ protein that consists of 6 transmembrane alpha helices.

A

Transmembrane.

37
Q

__________ is an enzyme that cleaves dietary into peptides.

A

Chymotrypsin.

38
Q

Chymotrypsin is produced by the _________ and secreted into the ____________.

A

Pancreas, Intestinal lumen.

39
Q

Chymotrypsin is composed of __________ beta barrels and ____________ short alpha helix.

A

Two and one.

40
Q

__________ is a fibrous protein mostly concentrated in muscle and connective tissue.

A

Collagen.

41
Q

Collagen is composed of a triple helix that contains __________, _____________, and ______________.

A

Glycine, proline, and hydroxyproline.

42
Q

____________ is a globular, tetrameric protein found in red blood cells.

A

Hemoglobin.

43
Q

Hemoglobin uses heme as a ___________ for each subunit.

A

Cofactor.

44
Q

Hemoglobin is a ____________ protein.

A

Transport.

45
Q

Collagen is a __________ protein.

A

Structural.

46
Q

_____________ are molecules of the immune system that recognize and bind to antigens.

A

Immunoglobulins.

47
Q

Immunoglobulins are __________ proteins.

A

Binding.

48
Q

____________ is a protein hormone produced by pancreatic beta cells.

A

Insulin.

49
Q

Interrupted or impaired insulin signaling can result in __________.

A

Diabetes.

50
Q

____________ diabetes is a failure to produce insulin.

A

Type I

51
Q

___________ diabetes insulin is not received.

A

Type II

52
Q

__________ acts as molecular motor in which energy is used to elicit a muscle contraction and transport vesicles in the cell.

A

Myosin.

53
Q

Myosin contains___________ chains and ____________ chains.

A

Heavy and light.

54
Q

_____________ chain interacts with the cytoskeletal protein_________.

A

Heavy, actin.

55
Q

__________ chain plays a role in binding Ca+2.

A

Light chains.

56
Q

Myosin is a _____________ protein.

A

Molecular motor.

57
Q

How many subunits does hemoglobin have?

A

4

Biochemistry (32 decks)

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