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Chapter 2: Proteins > Chapter 2: Proteins > Flashcards

Chapter 2: Proteins Flashcards

1
Q

Who is the swedish chemist that coined the term protein?

A

Jons Jacob Berzelius

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2
Q

What does the word protein was derived?

A

Proteios meaning first

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3
Q

What are the four elements of protein?

A

Carbon, hydrogen, oxygen, nitrogen

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4
Q

Does every protein contains 20 amino acids? Why or why not?

A

No, not every protein contains all 20 types of amino acids but most proteins contain most.

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5
Q

What do you call the common amino acids and why are the called as common amino acids?

A

a-amino acids because they have a primary amino group (-NH2) as a substituent of the a carbon atom, the carbon next to carboxylic acid group (-COOH)

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6
Q

What is the sole exception of a-amino acid? and why?

A

Proline because it has a secondary amino group (-NH-)

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7
Q

How does the 20 amino side chains differ?

A

differ in the structure of their side chains (R groups)

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8
Q

What is an amino acid?
draw or visualize its structure

A

a molecule that has an amine and carboxyl group

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9
Q

At physiological pH, what happens to amino and carboxylic acid?

A

Amino groups- protonated
Carboxylic acid groups - conjugated base (carboxylate) forms

Therefore, it can act both as an acid and base

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10
Q

What is dipolar ions or zwitterions?

A

This bear charged groups of opposite polarity.

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11
Q

Which is amino acids like other ionic compound more soluble?

A

Soluble more in polar solvent than in nonpolar solvents

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12
Q

What do you call the process in which amino acids can be polymerized to form chains and it is a bond formation with the elimination of a water molecule?

A

Condensation process

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13
Q

What do you call the resulting CO- NH linkage ( amide linkage)?

A

Peptide bond

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14
Q

What are these polymers composed of two, three, a few (3ā€“10), and many amino acid
units are known?

A

dipeptides, tripeptides, oligopeptides, and
polypeptides

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15
Q

After they are incorporated into a peptide, the individual
amino acids (the monomeric units) are referred to as amino acid _________?

A

residues

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16
Q

What do you call a residue with a a free amino group?

A

amino terminus or N-terminus

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17
Q

What do you call a residue with a a free carboxylate group?

A

carboxyl terminus or C-terminus

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18
Q

How to classify the amino acids?

A

polarities of their side chains

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19
Q

3 major types of amino acids

A

nonpolar R groups, uncharged polar R groups, charged polar R groups

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20
Q

What are the nine nonpolar amino acid?

A

GAVLIMPPT

Glycine
Aline
Valine
Leucine
Isoleucine
Methionine
Proline
Phenylalanine
Tryptophan

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21
Q

smallest possible side chain, as an H atom

A

Glycine

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22
Q

have aliphatic hydrocarbon atoms

A

Alanine, valine, leucine, and isoleucine

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23
Q

has a thioether side chain that resembles an n-butyl
group in many of its physical properties

A

Methionine

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24
Q

cyclic pyrrolidine side group.

A

Proline

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25
Q

it contains aromatic side groups

A

phenylalanine and tryptophan

26
Q

What does uncharged polar side chains have?

A

hydroxyl, amide, thiol groups

27
Q

What are the six amino acids classified as uncharged polar side chains

A

STATGC

Serine, Threonine, Asparagine, Glutamine, Tyrosine, Cysteine

28
Q

bear hydroxylic R groups of different sizes

A

Serine and Threonine

29
Q

amide-bearing
side chains of different sizes

A

Asparagine and Glutamine

30
Q

has a phenolic group

A

Tyrosine

31
Q

unique among the 20 amino acids in that it has a thiol
group that can form a disulfide bond with another cysteine through the oxidation of the two thiol groups

A

Cysteine

32
Q

how does disulfide bonds formed?

A

two thiol groups are oxidize

33
Q

The side chains of the acidic amino acids, aspartic acid and glutamic acid, are negatively
charged above pH 3; in their ionized state, they are often referred to _________ and ______- . Asparagine and glutamine are, respectively, the amides of aspartic acid and
glutamic acid

A

aspartate and
glutamate

34
Q

what are the essential amino acids?

A

ILVLMPTT

Isoleucine, Leucine, Valine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan

35
Q

Nonessential amino acids

A

AAACCGGGPST

Alanine, Arginine, Aspartic Acid, Cysteine, Cystine, Glutamic acid, Glutamine, Glycine, Proline, Serine, Tyrosine

36
Q

Arginine, Cysteine and Glutamine, along with Taurine may be considered conditionally essential. Why?

A

Their
requirements are
increased during periods
of catabolic stress.

37
Q

Disulfide bonds are one of the strongest
naturally-occurring bonds in nature. Disulfide
bonds link together two sulfur atoms attached
to ________ amino acids within the
polypeptide chains.

A

cysteine

37
Q

Disulfide bond formation
involves a reaction between the sulfhydryl
(SH) side chains of two cysteine residues

A

an
Sāˆ’ anion from one sulfhydryl group acts as a
nucleophile, attacking the side chain of a
second cysteine to create a disulfide bond,
and in the process releases electrons for
transfer

38
Q

Configuration and combination of proteins is several by several factors

A
  1. h-bonding (helical structure or pleated sheet)
  2. disulfide bonds
  3. salt bridges
  4. hydrophobic and hydrophilic tendencies
39
Q

proteins are bonds between oppositely
charged residues that are sufficiently close to each
other to experience electrostatic attraction

A

Salt bridges

40
Q

amino acid sequence of the protein

A

primary structure

41
Q

h-bonds in the peptide chain backbone; a-helix, b -sheets

A

secondary structure

42
Q

non-covalent interactions between the r groups within the protein

A

tertiary

43
Q

interaction between 2 polypeptide chains

A

quaternary sturtcure

44
Q

widely used in biochemical literature

A

three-letter abbreviations

44
Q

often used when comparing the amino acid sequences of several protein properties

A

one-letter symbol

45
Q

proteins turn like a spiral

A

a-helix

46
Q

proteins fold back on itself as in a ribbon

A

B-pleated sheet

47
Q

2 types of b sheets

A

anti-parallel (opposite)
parallel (same)

48
Q

class of shap; approximately spherical

A

Globular proteins

49
Q

parallel along a single axis (classes of shape)

A

Fibrous proteins

50
Q

Structure of proteins
- made up of amino acids joined together by peptide bonds

A

simple

51
Q
  • attached by covalent bonding or other intecations
A

cofactors and prosthetic groups

52
Q

composed of more that one subunit

A

oligomeric proteins

53
Q

prosthetic groups: metal ion
conjugated protein :

A

metalloprotein

54
Q

prosthetic groups: polysaccharides
conjugated protein :

A

glycoproteins

55
Q
A
56
Q

process by which peptide bonds are broken under acidic conditions and happens during digestion of proteins

A

protein hydrolysis

57
Q

involves the disruption and possible destruction of both the secondary and tertiary structure

A

denaturation of proteins

58
Q
A

Chapter 2: Proteins (1 decks)

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