Proteins & Enzymes Flashcards

(68 cards)

1
Q

These biomolecules contain many amide bonds, formed by joining amino acids.

A

Proteins

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2
Q

Proteins account for _____ of the dry weight of the human body.

A

50%

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3
Q

Unlike lipids and carbohydrates, proteins are ________ , so they must be ___________

A

not stored and must be consumed DAILY

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4
Q

How many grams of proteins should adult daily intake?

A

0.8 grams of protein per kg of body weight

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5
Q

Protein that stores O2 in tissues

A

Myoglobin

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6
Q

Protein hormones synthesized in the pancreas and controls blood glucose levels

A

Insulin

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7
Q

Transport protein that carries O2 in the blood

A

Hemoglobin

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8
Q

Protein that stores iron in the liver

A

Ferritin

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9
Q

Proteins that control muscle contractions

A

Actin and Myosin

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10
Q

This contain two functional groups—an amino group (NH2) and a carboxyl group (COOH).

A

Amino acids

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11
Q

The 20 amino acids that occur naturally in proteins differ in the identity of the R group bonded to the _________________.

A

alpha ( α) carbon

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12
Q

What is the simplest amino acid?
(R=H)

A

Glycine

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13
Q

The R group, called the ___________, determines the identity of the amino acid.

A

Side chain

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14
Q

It is basic amino acid if ___________

A

R = a basic N atom

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15
Q

If R = an additional COOH group, what amino acid is it?

A

Acidic amino acids

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16
Q

Since amino acids contain a base (NH2) and an acid (COOH), a proton transfers from the acid to the base to form?

A

Zwitterion

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17
Q

All amino acids (save glycine) have a ___________ on the α carbon.

A

Chiral center/chirality center

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18
Q

An amino acid exists as a _______________ zwitterion at a certain pH, the isoelectric pH.

A

Neutrally charged

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19
Q

When the pH _______ isoelectric pH, the carboxylate anion gains a proton, and the amino acid has a net positive charge.

A

less than

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20
Q

When the pH is GREATER than the isoelectric pH, the ammonium cation loses a proton, and the amino acid has a ____________

A

net negative charge

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21
Q

This and proteins are formed when amino acids are joined together by amide bonds.

A

Peptides

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22
Q

This is pentapeptides made in the brain, act as pain killers and sedatives by binding to pain receptors.

A

Enkephalins

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23
Q

Enkephalins belong to the family of polypeptides called ____________, which are known for their pain reducing and mood enhancing effects.

A

Endorphins

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24
Q

____________ and____________ are cyclic nonapeptide hormones, which have identical sequences except for two amino acids.

A

Oxytocin and Vasopression

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25
This stimulates the contraction of uterine muscles, and signals for milk production; it is often used to induce labor.
Oxytocin
26
It an antidiuretic hormone (ADH) targets the kidneys and helps to limit urine production to keep body fluids up during dehydration.
Vasopressin
27
What is the primary structure of a protein?
Sequence of amino acids
28
The secondary structure is the ______________________________________
3D arrangement of localized regions
29
These regions arise due to ______________________ between the N—H group of one amide with the C═O group of another.
Hydrogen bonding
30
The tertiary structure is the 3D shape adopted by _______________________
Peptide chain
31
The nonpolar side chains are stabilized by _______________________ forces in the interior of the structure.
London dispersion
32
Amino acids with charged side chains are attracted by?
Electrostatic interactions
33
The quaternary structure of the protein is the shape adopted when ___________ folded polypeptide chains come together into one complex.
Two or more
34
These are composed of long linear polypeptide chains that are bundled together to form rods or sheets.
Fibrous proteins
35
Fibrous proteins are _________ in water
Insoluble
36
These are coiled into compact shapes that are water SOLUBLE
Globular proteins
37
What are the globular proteins?
Enzymes and transport proteins
38
They are made of two mainly α-helix chains coiled around each other in a superhelix. They also found in hair, hooves, nails, skin, and wool.
α-Keratins
39
What vitamin that helps in stabilizing the chains? and when missing, poorly formed collagen fibers results.
Vitamin C
40
41
Myoglobin has ____ amino acids in 1 polypeptide chain
153
42
Hemoglobin has ____ polypeptide chains, each carrying a heme unit
Four (4)
43
Carbon monoxide (CO) is poisonous because it binds _______________ to the Fe2+ than does O2+
200 times more strongly
44
This is a disease where a single amino acid is different in two of the subunits of hemoglobin.
Sickle cell anemia
45
Protein hydrolysis involves ___________________ by treatment with aqueous acid, base, or certain enzymes.
breaking the peptide bonds
46
In the intestines, enzymes ________ and ________________ hydrolyze the remainder of the amide bonds resulting in individual amino acids.
trypsin and chymotrypsin
47
The process of altering the shape of a protein without breaking the amide bonds that form the primary structure.
Denaturation
48
What are the factors that can disrupt the non-covalent interactions that hold a protein in a specific shape.
High temperature Acid Base Agitation
49
These are proteins that serve as biological catalysts for reactions in all living organisms.
Enzymes
50
NAD+ is the ___________ that oxidizes lactate to pyruvate with the aid of the enzyme lactate dehydrogenase
cofactor (coenzyme)
51
An enzyme contains an ___________ that binds the substrate, forming an enzyme-substrate complex.
Active site
52
The energy difference between reactants and the formation of products
Free energy of activation
53
This model states that the active site is a RIGID CAVITY; to react, the substrate must exactly match the shape of the active site.
Lock-and-key model
54
This model states that the active site has a FLEXIBLE SHAPE, which can adjust to fit a variety of substrate shapes.
Induced-fit model
55
This bonds to the enzyme and alters or destroys the enzyme’s activity
Inhibitor
56
A _________________ inhibitor has a shape and structure similar to the substrate, so it competes with the substrate for binding to the active site.
Competitive
57
A ______________________ inhibitor bonds to the enzyme, but not to the active site.
Noncompetitive
58
These are an inactive form of an enzyme that can be converted to the active form when needed.
Zymogens (proenzymes)
59
This inhibits the enzyme that forms cell walls of bacteria, destroying the bacterium.
Penicillin
60
ACE causes blood vessels to narrow, increasing blood pressure. What is ACE?
Angiotensin-converting enzyme
61
These are given to those with high blood pressure to prevent ACE’s synthesis from it’s zymogen.
ACE inhibitors
62
An essential enzyme that allows the virus to make copies of itself.
HIV protease
63
HIV protease inhibitors interfere with this copying, ___________ the virus population in the patient.
Decreasing
64
Factor affecting enzymes activity
Not limited to: - Temperature and pH - Enzyme and Substrate concentration - Cofactors - Inhibitors
65
If the temperature exceeds the optimum temperature, the enzyme will be ______________
denatured
66
The pH usually ranges between __ to __. Marked changes in pH produce conformational changes in protein structures that result in decreased activity
5 to 9
67
The velocity of the reaction increases as the ENZYME concentration increases up to a certain point where the enzyme is saturated with substrate.
Enzyme concentration
68
The velocity of the reaction increases as the SUBSTRATE concentration increases up to a point where the enzyme is saturated with the substrate.
Substrate concentration