Post Lab Exp 2: Protein Denaturation Flashcards

1
Q

What are the objectives of the Exp 2: Protein Denaturation

A

❏ To observe the effects of several denaturing reagents on a
protein sample
❏ To differentiate the effect of these denaturing reagents to the
protein sample
❏ To cite practical applications of these denaturing agents.

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2
Q

Any modification in conformation not accompanied by rupture of peptide
bonds

A

Protein Denaturation

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3
Q

Involves the disruption and possible destruction of both the secondary
and tertiary structures

A

Protein Denaturation

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4
Q

Loss of Biological Activity of Protein

A

Denaturation

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5
Q

Regains Activity of Protein

A

Renaturation

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6
Q

The sequence of amino acids present in protein’s peptide chain or chains

A

Primary Structure

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7
Q

The regularly repeating ordered spatial arrangements amino acids near each other in the protein chain.

A

Secondary Chain

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8
Q

What are the Secondary Structure of Proteins

A

Alpha Helix
Beta Pleated Sheet

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9
Q

The overall three-dimensional shape that results from the attractive forces between amino acid side chains

A

Tertiary Structure

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10
Q

Types of chemical bonds that are targeted by denaturing agents In secondary structures –

A

hydrogen bonds are disrupted

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11
Q

In tertiary structure there
are four types of bonding
interactions between “side
chains” including

A

❏ hydrogen bonding
❏ salt bridges
❏ disulfide bonds
❏ and non-polar hydrophobic
interactions

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12
Q

Effects of Denaturation

A

❏ Decreased solubility
❏ Altered water binding capacity
❏ Loss of biological activity
❏ Destruction of toxins
❏ Improved digestibility
❏ Increased intrinsic viscosity
❏ Inability to crystallize

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13
Q

Denaturing Agents

A

Heat
Alcohol
Strong Acids and Strong Bases
Heavy Metals
Alkaloidal reagent

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14
Q

increases the kinetic
energy and causes the
molecules to vibrate so rapidly
and violently that the bonds
are disrupted

A

Heat

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15
Q

Disrupts hydrogen
bonding
■ Denatures both
secondary and tertiary
structures

A

Alcohol

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16
Q

also reducing agents/oxidizing agents that can disrupt the disulfide bonds in
protein structure.

salts are ionic, they disrupt salt bridges in proteins or replaces one metal with another

A

Heavy Metals

17
Q

disrupt salt bridges held together by ionic charges that can affect the
environmental pH of proteins.

A

acids and bases

18
Q

High molecular weight
anions
■ The negative charge of
these anions counteracts
the positive charge of the
amino group in proteins
disrupting salt bridges

A

Alkaloidal reagent

19
Q
A