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Biochemistry > Proteins > Flashcards

Proteins Flashcards

1
Q

_____________ are the major structural and functional components of all cells in the body, and act to facilitate biochemical reactions among the most abundant biological macromolecules and are extremely versatile in their functions.

A

Proteins

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2
Q

Proteins play a crucial role in a healthy, balanced diet. For example, without sufficient protein nutrition, we would not be able to form ________, and the body’s ability to repair and generate cells would be affected.

A

enzymes

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3
Q

____________ percent of the human body is made up of proteins.

A

Twenty

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4
Q

A typical human cell contains about __________ different kinds of proteins, and the human body contains about ________ different proteins.

A

9000, 100 000

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5
Q

All proteins contain the elements _______, _________, __________, and __________; most also contain ______.

A

carbon, hydrogen, oxygen, nitrogen, sulfur

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6
Q

Proteins are composed of ___________ carbon.

A

50-55%

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7
Q

Proteins are composed of ___________ carbon.

A
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8
Q

Proteins are composed of ___________ oxygen.

A

19-24%

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9
Q

Proteins are composed of ___________ nitrogen.

A

13-19%

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10
Q

Proteins are composed of ___________ sulfur.

A

0-4%

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11
Q

The building blocks for Proteins

A

Amino acids

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12
Q

It is a molecule that has both negative and positive charges

A

Zwitterion

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13
Q

Amino acids are _____________ (able to react both as
a base and as an acid.)

A

amphoteric

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14
Q

Amino acids naturally occur in ___ form

A

L

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15
Q

It is a molecule that has a positive charge on
one atom and a negative charge on another atom, but
which has no net charge.

A

Zwitterion

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16
Q

In an acidic solution, the zwitterion accepts a _________ to form a positively charged ion.

A

proton (H+
)

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17
Q

In basic solution, the -NH3 of the zwitterion _______ a proton,
and a negatively charged species is formed.

A

loses

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18
Q

___________ are the best-known examples of zwitterions.

A

Amino acids

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19
Q

Classification of Amino Acids based on Side Chain (R groups)

A
  1. Non polar aliphatic amino acids
    2.Amino acids with Uncharged (neutral) side chain
  2. Acidic amino acids
    4.Amino acids with basic side chain
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20
Q

Classification of Amino Acids Based on Capacity of the Body to Synthesize Them

A
  1. Essential Amino acids
  2. Non-essential amino acids
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21
Q

There are _____ essential amino acids

A

nine

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22
Q

There are ________ essential amino acids

A

eleven

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23
Q

They cannot be synthesized in the body and, therefore, must be present in the diet in order for protein synthesis to occur.

A

Essential amino acids

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24
Q

It is required for growth in children but is not an essential amino acids for adults

A

Arginine

25
Q

These amino acids can be synthesized in the body itself and hence not necessarily needed to be acquired through diet

A

Non-essential Amino Acids

26
Q

Amino acids are linked together in proteins by a special kind of bond

A

Peptide bonds

27
Q

Small Peptide Hormones

A

o Vasopressin
o Oxytocin

28
Q

Small Peptide Neurotransmitters

A

Enkephalins

29
Q

Small Peptide Antioxidants

A

Glutathione

30
Q

___________ regulates the excretion of water by the kidneys; it also affects blood pressure

A

Vasopressin

31
Q

Another name for vasopressin is _________________

A

antidiuretic hormone (ADH)

32
Q

It is produced by the pituitary gland, and stimulates uterine contractions in labor.

A

Oxytocin

33
Q

It was the first naturally-occurring hormone to be produced in a laboratory.

A

Oxytocin

34
Q

Pentapeptide neutrotransmitters produced by the brain itself that bind at the receptor sites in the brain to reduce pain.

A

ENKEPHALINS

35
Q

Is present in significant concentrations in most cells and have physiological importance as a regulator of oxidation-reduction reactions. As anti-oxidants. Protecting cells contents form the oxidizing agents such as peroxides and superoxides.

A

Glutathione

36
Q

They are examples of chemical signaling peptides. They are natural painkillers that are produced in the body. They interact with receptors in the brain to inhibit the transmission of pain signals.

A

Endorphins

37
Q

___________ is a naturally occurring, extremely complex substance that consists of amino acid residues joined by peptide bonds

A

Protein

38
Q

4 PROTEIN STRUCTURAL LEVELS

A

•PRIMARY STRUCTURE
•SECONDARY STRUCTURE
•TERTIARY STRUCTURE
•QUATERNARY STRUCTURE

39
Q

Is the order in which amino acids are linked together in a protein.

A

Primary Structure

40
Q

The hormone that regulates blood
glucose levels

A

Insulin

41
Q

Is the arrangement in a space adopted by the backbone portion of protein.

A

Secondary structure

42
Q

The polypeptide chain is coiled tightly in the fashion of a spring

A

Alpha helix

43
Q

In this structure, individual protein chains are aligned side-by-side with every other protein chain aligned in an opposite direction.
The protein chains are held together by intermolecular hydrogen bonding, that is hydrogen bonding between amide groups of two separate chains.

A

Beta pleated sheets

44
Q

Is the overall three dimensional structure shape of the protein that result from the interaction between amino acid side chains (R Groups).

A

Tertiary structure

45
Q

it is the strongest of the tertiary structure interactions result from the –SH groups. Of two cysteine residues interacting with each other forming

A

Covalent Disulfide

46
Q

Involves the interactions between the acidic side Groups and basic R group. The acidic being negative
–COOH becomes –COO-
The basic being positive –NH2 becomes NH3 +

A

Electrostatic interactions called salt
bridges

47
Q

This can occur between amino acids with polar R groups.

A

Hydrogen bonds

48
Q

Results when 2 non polar amino acids are close with each other.

A

HYDROPHOBIC INTERACTIONS

49
Q

Highest level of protein organization. It is only found in multimeric proteins. Describes the
interactions of the subunits in an oligomeric protein. Present also
the electrostatic
interactions
Hydrogen bonds

A

Quaternary structure

50
Q

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

A

Primary Structure

51
Q

The regularly repeating ordered spatial arrangements of amino acids near each other in the protein chain, which result from hydrogen bonds between carbonyl oxygen atoms and amino hydrogen atoms

A

Secondary structure

52
Q

The overall three-dimensional shape that results from the attractive forces between amino acid side chains (R groups) that are not near each other in the protein chain

A

Tertiary structure

53
Q

The three-dimensional shape of a protein consisting of two or more independent peptide chains, which results from noncovalent interactions between R groups

A

Quaternary structure

54
Q

3 Main types of proteins

A

Fibrous, Globular, and Conjugated

55
Q

It 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.

A

Fibrous proteins

56
Q

A __________ is a protein whose molecules have peptide chains that are folded into spherical or globular shapes.

A

globular protein

57
Q

These are simple proteins combined with some non-protein material in the body.

A

Conjugated proteins

58
Q

____________ is a structural change in a protein that results in the loss (usually permanent) of its biological properties

A

Denaturation

59
Q

Temperatures at which proteins denature may vary, but most human proteins function optimally at body temperature (~37ºC).

A

True

Biochemistry (11 decks)

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