Protein Hydrolysis—Protein Classification Based on Shape Flashcards

1
Q

When a protein or smaller peptide in a solution of strong acid or strong base
is heated, the peptide bonds of the amino acid chain are __________ and free
amino acids are produced. The ___________ is the reverse of the formation
reaction for a peptide bond.

A

hydrolyzed/hydrolysis reaction

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2
Q

Often, for limited denaturation changes, it is possible to find conditions under which the effects of denaturation can be reversed; this _________________, in which the protein is “refolded,” is called renaturation.

A

restoration process

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3
Q

Loss of water solubility is a frequent physical consequence of protein denaturation. The precipitation out of biochemical solution of denatured protein is called _______________.

A

coagulation

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4
Q

In surgery, heat is often used to seal small blood vessels. This process is called _____________.

A

cauterization

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5
Q

A temperature above _____________ is extremely
dangerous, as the body’s enzymes begin to be inactivated at this level.

A

1068F (418C)

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6
Q

disrupts hydrogen bonds by making molecules
vibrate too violently; produces coagulation, as in
the frying of an egg

A

heat

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7
Q

causes violent vibrations of molecules that disrupt hydrogen bonds

A

Microwave radiation

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8
Q

operates very similarly to the action of heat (e.g.,
sunburning)

A

UV radiation

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9
Q

causes molecules in globular shapes to extend to longer lengths, which then entangle (e.g., beating
egg white into meringue)

A

violent whipping or shaking

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10
Q

affects R-group interactions

A

detergent

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11
Q

interferes with R-group interactions because these solvents also can form hydrogen bonds; quickly denatures proteins in bacteria, killing them (e.g., the disinfectant action of 70% ethanol)

A

organic solvents (e.g., ethanol, 2-propanol, acetone)

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12
Q

disrupts hydrogen bonds and salt bridges;
prolonged action leads to actual hydrolysis of
peptide bonds

A

strong acids and bases

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13
Q

metal ions combine with ㅡSH groups and form
poisonous salts

A

salts of heavy metals (e.g., salts of Hg2+, Ag+, Pb21+)

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14
Q

reduces disulfide linkages to produce 9SH groups

A

reducing agent

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15
Q

A ____________ is a protein whose molecules have an elongated shape with one dimension much longer than the others. They tend to have simple, regular, linear structures. There is a tendency for such proteins to aggregate together to form macromolecular structures.

A

fibrous protein

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16
Q

A ______________ is a protein whose molecules have peptide chains that are folded into spherical or globular shapes. Generally, these are water-soluble substances.

A

globular protein

17
Q

A _______________ is a protein that is found associated with a membrane system of a cell. Thus, such proteins tend to be water-insoluble and they usually have fewer hydrophobic amino acids than globular proteins.

A

membrane protein

18
Q

It is the major protein constituent of hair, feathers, wool, fingernails and toenails, claws, scales, horns, turtle shells, quills, and hooves.

A

a-keratin

19
Q

Introduction of _____________ within the several levels of coiling structure determines the “hardness” of an a-keratin.

A

disulfide bridges

20
Q

____________, the most abundant of all proteins in humans (30% of total body protein), is a major structural material in tendons, ligaments, blood vessels, and skin; it is also the organic component of bones and teeth.

A

Collagen

21
Q

The globular protein ___________ transports oxygen from the lungs to tissue.

A

hemoglobin

22
Q

The globular protein ___________ functions as an oxygen storage molecule in muscles. It consists of a single peptide chain and a heme unit, and hemoglobin has four peptide chains and four heme units. Thus only one O2 molecule can be carried by this molecule.

A

myoglobin