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Biochemistry LAB > Lesson 2: Reactions and Stability of Proteins > Flashcards

Lesson 2: Reactions and Stability of Proteins Flashcards

1
Q

Protein Structure: two dimensional (length and height)

A

Primary

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2
Q

Protein Structure: three-dimensional spatial arrangement (around the carbon chain/skeleton)

A

Secondary

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3
Q

Protein Structure: shape in which the entire protein chain folds together in three-dimensional space

A

Tertiary

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4
Q

Protein Structure: two or more folded protein chains come together to form a ‘superstructure’

A

Quaternary

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5
Q

__________ and __________ interactions contribute to the structure of proteins, mainly their __________.

A

Peptide bonds; side chain; tertiary structure

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6
Q

The form is determined mainly by their _________ and is stabilized by _________ and _________ .

A

amino acid sequence; inter-chain; intra-chain hydrogen bonding

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7
Q

Side chains of various amino acids may also interact via the following

A
  1. Hydrogen Bonding
  2. Hydrophobic Interactions
  3. Salt Bridges
  4. Disulphide Bridges
  5. Dipole-Dipole and Ion-Dipole Forces
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8
Q

The amino acid sequences greatly affect the _____________ of proteins.

A

physico-chemical properties

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9
Q

physico-chemical properties of proteins

A
  1. Solubility
  2. Molecular weight
  3. Shape
  4. Isoelectric pH
  5. Precipitation
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10
Q

__________ is the term used for any change in the three-dimensional structure of a protein that renders it incapable of performing its
assigned function.

A

Denaturation

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11
Q

Denaturation: Physical means

A

heat,
violent shaking,
very high pressures,
UV radiation

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12
Q

Denaturation: Chemical means

A

pH,
high salt concentrations,
heavy metal ions,
organic solvents,
surface active agents,
high concentrations of urea.

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13
Q

Displays number and types of amino acids and number of peptide chains

A

Primary

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14
Q

Bonds involved in primary

A

H-bonds

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15
Q

Bonds involved in Secondary

A

Functional <-> R group

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16
Q

Bonds involved in Quarternary

A

(Functional <-> R group) 2 or more

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17
Q

Salt bridges other name

A

Electrostatic interaction

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18
Q

cysteine residue thiol group + another cysteine residue thiol group

A

Disulfide Bridges (Intra)

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19
Q

Primary Structure maintained by _______, peptide bonds

A

covalent

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20
Q

Any change in the ________ of amino acids may cause abnormal function of the polypeptide.

A

sequence

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21
Q

__________ is caused by the change in amino acid sequence of __________

A

Sickle anemia; hemoglobin

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22
Q

Hemoglobin in sickle cell anemia lacks ________and has ________ instead

A

Glutamate; valine

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23
Q

arrangement in space adopted by the backbone portion of a protein

A

Secondary Structure

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24
Q

Backbone portion of amino acids

A

Amino group
cardial Carbon
Carboxylic group
Hydrogen

25
Q

coiled shape held in place by hydrogen bonds between the amide groups (-NH) and the carbonyl (-C=O) groups attached to the α-carbon.

R groups are not involved in this level of structure.

A

alpha helix (α-helix)

26
Q

consists of polypeptide chains arranged side by side

held together by hydrogen bonding between the amine and the carbonyl oxygen within the amino acid backbone.

A

beta-pleated sheet (β-pleated sheet)

27
Q

results from the interactions between amino acid side chains that are widely separated from each other within a peptide chain.

A

Tertiary Structure

28
Q

three-dimensional spatial “arrangements”

A

secondary structures of proteins

29
Q

specific three-dimensional “shape”

A

tertiary structure of a protein

30
Q

Side chain <-> Side chain

A

Hydrogen bonding

31
Q

relatively weak and are easily disrupted by changes in pH and temperature.

A

Hydrogen bonding (Intra)

32
Q

Nonpolar side-chains are attracted to other nonpolar side-chains

“water-free pockets” in the interior region

nonpolar R groups aggregate in the interior portion of the polypeptide chain, leaving the polar portion in the exterior.

A

Hydrophobic interactions (inter)

33
Q

Hydrophobic interactions (inter) example

A

London forces

34
Q

between an acidic side chain (R group) and a basic side chain (R group)

A

Electrostatic interaction/Salt bridges (Intra)

35
Q

highest level of protein organization

found only in multimeric proteins

two or more peptide chains

A

Quaternary structure

36
Q

Quaternary structure Example:

A

hemoglobin

37
Q

(two subunits

A

dimer

38
Q

four subunits

A

tetramer

39
Q

Color and Taste

A

colourless and usually tasteless

40
Q

Shape and Size

A

simple crystalloid spherical structures to long fibrillar structures.

41
Q

globular

A

(insulin)

42
Q

oval

A

(albumin)

43
Q

fibrous or elongated

A

(fibrinogen)

44
Q

Solubility

A

▪ influenced by pH
▪ lowest at isoelectric point

45
Q

__________ instead of true solutions in water

A

colloidal solutions

46
Q

Molecular weight

A

110

47
Q

Molecular weight majority of proteins/polypeptides:

A

40 to 4,000 amino acids

48
Q

molecular weight Insulin

A

5,700

49
Q

molecular weight Myoglobin

A

17,000

50
Q

molecular weight Hemoglobin

A

64,450

51
Q

Molecular weight Serum albumin

A

69,000

52
Q

Precipitate

A

Flocculum

53
Q

act as acids and alkali

A

Amphoteric

54
Q

can form salts with both cations and anions based on their net charge

A

Ion binding capacity

55
Q

Pepsin (pI) -

A

1.1

56
Q

Casein (pI)

A

4.6;

57
Q

Human albumin (pI)

A

4.7;

58
Q

Urease (pI)

A

5.0;

59
Q

Hemoglobin (pI)

A

6.7;

Biochemistry LAB (5 decks)

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