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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

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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

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3
Q

For transport of other substances
(ex. hemoglobin)

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

A

B. Transport

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4
Q

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

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

A

D. Receptor

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5
Q

For movement
(ex. myosin, actin)

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

A

C. Contractile

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6
Q

for protection against disease
(ex. antibodies)

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

A

B. Defensive

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7
Q

For hastening biochemical reactions
(ex. amylase)

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

A

B. Catalytic

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8
Q

For support (ex. collagen, elastin)

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

A

A. Structural

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9
Q

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

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

A

C. Storage

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10
Q

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

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

A

A. Regulation

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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

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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

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13
Q
  • Lysine (Lys, K): ε-amino group
  • Arginine (Arg, R): guanidino group
  • Histidine (His, H): imidazole group
A

Basic amino acids

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14
Q
  • Aspartic acid (Asp, D): β-carboxylate
  • Glutamic acid (Gln, E): γ-carboxylate
A

Acidic amino acids

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15
Q

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

A

Arginine & Histidine

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16
Q

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

A

Tyrosine

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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

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18
Q

The most common configuration of amino acids and naturally occurring

A

L-configuration

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19
Q

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

A

a-carbon and chiral

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20
Q

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

A

Different pKa

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21
Q

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

A

Chiral

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22
Q

Amino acids may act within an aqueous environment.

A

Weak acids and bases

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23
Q

Aside from the ionizable carboxyl and amino groups, the ___

A

Side chains may also be ionized at varying pH

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24
Q

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

A

Tryptophan (2.43)

25
What is the lowest value of pKa Ca-COOH in amino acids?
Cysteine (1.71)
26
What is the highest value of pKa (Ca-NH3) in amino acids?
Cysteine (10.78)
27
What is the lowest value of pKa (Ca-NH3) in amino acids?
Asparagine (8.80)
28
What is the highest value of pKa side chain in amino acids?
Arginine (12.48)
29
What is the lowest value of pKa side chain in amino acids?
Aspartic acid (3.86)
30
What is the highest value of Isometric point (PI) in amino acids?
Arginine (10.76)
31
What is the lowest value of Isometric point (PI) in amino acids?
Aspartic acid (2.98)
32
pH at which amino acid attains its zwitterion form
ISOELECTRIC pH (pI)
33
A neutral molecule with both positive and negative electrical charges.
Zwitterion
34
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.
Dissociation of the hydrogen
35
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
Peptide bond
36
Beginning of the protein where free – NH3+ group
N-terminal end
37
End of the protein where –COO- group
C-terminal end
38
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
Primary Structure
39
Vasopressin and Oxytocin are both?
Nonapeptides
40
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
Secondary structure
41
The most common type of secondary structure
α-Helix β-Pleated sheet
42
* Spiral structure * Stabilized by intramolecular H-bonds * All R groups point outward from the helix Example: Keratin present in hair and skin
α-Helix
43
Structural features of α-Helix
* 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
Advance within one complete rotation
Pitch
45
Advance per amino acid
Rise
46
Between successive charged aa residues.
Electrostatic repulsion (or attraction)
47
Between adjacent R-groups
Bulkiness (steric strain)
48
Formed when 2 or more polypeptides line side-by-side Stabilized by hydrogen bonds (intrachain or interchain) of adjacent polypeptide chains
β-Pleated Sheets
49
Structural feature of β-Pleated Sheets
* β-strands are extended into a zigzag * All R groups extend above or below the sheet in an alternating up-and-down direction
50
* Run in opposite directions * Forms linear H-Bonds (stronger)
ANTI-PARALLEL β-Pleated Sheets
51
* Run in the same directions * Forms bent H-Bonds (weaker)
PARALLEL β-Pleated Sheets
51
* 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
Tertiary Structure
52
* 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
Fibrous proteins
53
* 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.)
Globular proteins
54
Refers to the spatial arrangement of polypeptide subunits Subunits are stabilized by non-covalent interactions (like 3 degrees structure)
Quaternary Structure
55
Refers to a change in protein native conformation 🡪 disrupts protein function Loss of 2o, 3o, and 4o structures
Protein denaturation
56
* High temperature * Vigorous shaking or agitation * Hydrostatic pressure * UV radiation
Physical agents
57
* 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
Chemical agents
58
Physical agent -> Chemical agent
PROTEIN DYSFUNCTION

Biochemistry (17 decks)

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