Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Biochemistry > Protein > Flashcards

Protein Flashcards

1
Q

The spatial arrangement of atoms in a protein.

A. Native conformation
B. Conformation
C. Protein
D. Loss of biological function

A

B. Conformation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

3-D folded conformation with active function

A. Native conformation
B. Conformation
C. Protein
D. Loss of biological function

A

A. Native conformation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

For transport of other substances
(ex. hemoglobin)

A. Structural
B. Transport
C. Regulation
D. Receptor

A

B. Transport

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

For the response of cells to external stimuli
(ex. neuron receptors)

A. Structural
B. Transport
C. Regulation
D. Receptor

A

D. Receptor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

For movement
(ex. myosin, actin)

A. Structural
B. Transport
C. Contractile
D. Receptor

A

C. Contractile

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

for protection against disease
(ex. antibodies)

A. Structural
B. Defensive
C. Contractile
D. Receptor

A

B. Defensive

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

For hastening biochemical reactions
(ex. amylase)

A. Structural
B. Catalytic
C. Storage
D. Transport

A

B. Catalytic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

For support (ex. collagen, elastin)

A. Structural
B. Catalytic
C. Storage
D. Transport

A

A. Structural

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

For storage of amino acids
(ex. casein, ovalbumin)

A. Structural
B. Catalytic
C. Storage
D. Transport

A

C. Storage

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

For regulation of bodily activities
(ex. insulin, glucagon)

A. Regulation
B. Catalytic
C. Storage
D. Transport

A

A. Regulation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q
  • Glycine (Gly, G): hydrogen
  • Alanine (Ala, A): methyl group
  • Valine (Val, V): isopropyl group
  • Isoleucine (Ile, I): sec-butyl group
  • Leucine (Leu, L): isobutyl group
  • Proline (Pro, P): cyclic structure
  • Phenylalanine (Phe, F): benzyl group
  • Methionine (Met, M): thioether group
  • Tryptophan (Trp, W): indole group
A

Non-polar acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q
  • Serine (Ser, S): primary alcohol group
  • Threonine (Thr, T): secondary alcohol
  • Cysteine (Cys, C): thiol group
  • Asparagine (Asn, N)
  • Glutamine (Gln, Q)
  • Tyrosine (Tyr, Y): phenolic group
A

Polar uncharged

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q
  • Lysine (Lys, K): ε-amino group
  • Arginine (Arg, R): guanidino group
  • Histidine (His, H): imidazole group
A

Basic amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q
  • Aspartic acid (Asp, D): β-carboxylate
  • Glutamic acid (Gln, E): γ-carboxylate
A

Acidic amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

This is essential in the diets of juveniles, not adults.

A

Arginine & Histidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

It is classified as nonessential only because it is readily formed from essential phenylalanine.

A

Tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

True or False;

Amino acids are important for growth and normal body functioning but cannot be synthesized by the body. Hence, must be obtained from the diet.

A

True

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

The most common configuration of amino acids and naturally occurring

A

L-configuration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

With the exception of Glycine, all protein-derived amino acids have at least one stereocenter

A

a-carbon and chiral

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Different functional groups gain and lose their electrons/H atoms at various pH, and therefore have

A

Different pKa

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Optically active carbon center; carbon atom that has four different substituents

A

Chiral

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Amino acids may act within an aqueous environment.

A

Weak acids and bases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Aside from the ionizable carboxyl and amino groups, the ___

A

Side chains may also be ionized at varying pH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What is the highest value of pKa (Ca-COOH) in amino acids?

A

Tryptophan (2.43)

25
Q

What is the lowest value of pKa Ca-COOH in amino acids?

A

Cysteine (1.71)

26
Q

What is the highest value of pKa (Ca-NH3) in amino acids?

A

Cysteine (10.78)

27
Q

What is the lowest value of pKa (Ca-NH3) in amino acids?

A

Asparagine (8.80)

28
Q

What is the highest value of pKa side chain in amino acids?

A

Arginine (12.48)

29
Q

What is the lowest value of pKa side chain in amino acids?

A

Aspartic acid (3.86)

30
Q

What is the highest value of Isometric point (PI) in amino acids?

A

Arginine (10.76)

31
Q

What is the lowest value of Isometric point (PI) in amino acids?

A

Aspartic acid (2.98)

32
Q

pH at which amino acid attains its zwitterion form

A

ISOELECTRIC pH (pI)

33
Q

A neutral molecule with both positive and negative electrical charges.

A

Zwitterion

34
Q

At low pH, both of the amino and carboxyl groups are fully protonated. As the pH of the solution is raised, the –COOH group of Form I can ionize and donate H+ to the medium. The release of the proton results to carboxylate group, -COO-. The Form II then has a net charge of zero.

A

Dissociation of the hydrogen

35
Q

The “workhorses” of biological systems

Large biomolecules made of amino acids joined by amide bonds called

The special name given to the amide covalent bond between the α-carboxyl group of one amino acid and the α-amino group of another amino acid

A

Peptide bond

36
Q

Beginning of the protein where free – NH3+ group

A

N-terminal end

37
Q

End of the protein where –COO- group

A

C-terminal end

38
Q

The sequence of amino acids in a polypeptide chain

The number of peptides possible from 20 protein-derived amino acids is enormous

The number of peptides possible for a chain of n amino acids is 20n

For a small protein of 60 aa, 2060 is a possible number of protein

A

Primary Structure

39
Q

Vasopressin and Oxytocin are both?

A

Nonapeptides

40
Q

Refers to the ordered 3D arrangements in localized regions of a polypeptide chain (regular folding)

Formed and stabilized by a hydrogen bond between the amide proton and carbonyl oxygen

A

Secondary structure

41
Q

The most common type of secondary structure

A

α-Helix
β-Pleated sheet

42
Q
  • Spiral structure
  • Stabilized by intramolecular H-bonds
  • All R groups point outward from the helix

Example: Keratin present in hair and skin

A

α-Helix

43
Q

Structural features of α-Helix

A
  • C=O of each peptide bond is hydrogen bonded to the N-H of the fourth amino acid away; there are 3.6 aa/turn
  • Pitch: 0.54nm
44
Q

Advance within one complete rotation

A

Pitch

45
Q

Advance per amino acid

A

Rise

46
Q

Between successive charged aa residues.

A

Electrostatic repulsion (or attraction)

47
Q

Between adjacent R-groups

A

Bulkiness (steric strain)

48
Q

Formed when 2 or more polypeptides line side-by-side

Stabilized by hydrogen bonds (intrachain or interchain) of adjacent polypeptide chains

A

β-Pleated Sheets

49
Q

Structural feature of β-Pleated Sheets

A
  • β-strands are extended into a zigzag
  • All R groups extend above or below the
    sheet in an alternating up-and-down
    direction
50
Q
  • Run in opposite directions
  • Forms linear H-Bonds (stronger)
A

ANTI-PARALLEL β-Pleated Sheets

51
Q
  • Run in the same directions
  • Forms bent H-Bonds (weaker)
A

PARALLEL β-Pleated Sheets

51
Q
  • Refers to the three-dimensional conformation of the entire polypeptide
  • Stabilized by numerous interactions between amino acid side chains
    • Covalent bonds
    • H-bonds
    • Salt bridges (electrostatic)
    • Hydrophobic interaction
A

Tertiary Structure

52
Q
  • Contain polypeptide chains organized approximately parallel along a single-axis
  • Structural features:
    • Consist of long fibers or large sheets
    • Tend to be mechanically strong
    • Insoluble to water
    • Play important structural roles
A

Fibrous proteins

53
Q
  • Proteins are folded to a spherical shape
  • Structural features:
    • Most of the polar side chains are on the outside;
      nonpolar side chains buried inside the structure
    • Soluble to water
    • Nearly all have substantial sections of α-helix and
      β-sheet
    • Function: metabolic (catalytic, transport, etc.)
A

Globular proteins

54
Q

Refers to the spatial arrangement of polypeptide subunits

Subunits are stabilized by non-covalent interactions (like 3 degrees structure)

A

Quaternary Structure

55
Q

Refers to a change in protein native conformation 🡪 disrupts protein function

Loss of 2o, 3o, and 4o structures

A

Protein denaturation

56
Q
  • High temperature
  • Vigorous shaking or agitation
  • Hydrostatic pressure
  • UV radiation
A

Physical agents

57
Q
  • Change in pH
  • Change in ionic strength
  • Organic solvents (e.g. urea, alcohol)
  • Reducing agents (e.g. performic acid and mercaptoethanol)
  • Detergents
  • Salts of heavy metals
A

Chemical agents

58
Q

Physical agent -> Chemical agent

A

PROTEIN DYSFUNCTION

Biochemistry (17 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions