PROTEINS Flashcards

1
Q

Chemistry of Life

A

Biochemistry

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2
Q

A natural science concerned with the study of life and living organisms

A

Biology

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3
Q

Seeks to describe the structurr, organization, and functions of living matter in molecular terms

A

Biochemistry

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4
Q

Organisms which lack one or more functional conponents with respect to the so-called “wild type” or normal phenotype

A

Mutants

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5
Q

2 Basic Classifications of Organisms

A

• Procaryotes
•Eucaryotes

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6
Q

Simple unicellular organisms, mainly bacteria and blue green algae

A

Procaryotes

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7
Q

Organisms including plants and animals

A

Eucaryotes

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8
Q

The fluid part of cytoplasm

A

Cytosol

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9
Q

How many lercent of water is in the human body?

A

70% of water

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10
Q

4 Biomolecules:

A

• Proteins
•Lipids
•Carbohydrates
•Nucleic Acids

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11
Q

Attractive forces that holds molecules together

A

Intermolecular Forces (IMF)

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12
Q

What do you call the states of matter?

A

Consequence

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13
Q

Strong IMF

A

Solid

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14
Q

Weak IMF

A

Gas

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15
Q

Moderate IMF

A

Liquid

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16
Q

A large unbranched naturally occuring biomolecule made up of numerous amino acids linked by amide bonds

A

Protein

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17
Q

Most abundant molecules in the cells after water

A

Proteins

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18
Q

How many percent is protein in a cell’s overall mass?

A

15%

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19
Q

What elements are always present in protein?

A

• Carbon (C)
•Hydrogen (H)
•Nitrogen (N)
•Oxygen (O)
•Some: Sulfur (S)

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20
Q

Some functions of protein:

A

• Structure
• Catalysts
•Hormones
• Protection
• Movement
• Transport
• Storage
• Regulation

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21
Q

2 Major types of proteins:

A

Globular and Fibrous

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22
Q

Proteins that are soluble in water but are non structural

A

Globular Proteins

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23
Q

Proteins that are insoluble in water but structural

A

Fibrous

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24
Q

What is the average nitrogen content by mass in protein?

A

15.4% by mass

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25
Q

A compound that contains both an amino group and a carboxyl group

A

Amino acid

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26
Q

Building blocks of proteins

A

Amino acid

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27
Q

How many primordial amino acids are there?

A

20

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28
Q

T OR F:
All amino acids are in the a-L configuration

A

True

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29
Q

How many standard amino acids contain a chiral center?

A

19/20

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30
Q

The COOH is put at the top

A

Fischer Projection

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31
Q

Positioning NH2 on the left

A

L-Isomer

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32
Q

Positioning NH2 on the right

A

D-Isomer

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33
Q

T OR F:
When not in pure form, amino acids are white crystalline solids.

A

False (Pure form.)

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34
Q

What are incorporated into polypeptides during protein synthesis?

A

20 Primordial amino acids

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35
Q

How many aliphatic R groups are there?

A

7

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36
Q

How many polar R groups are there?

A

5

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37
Q

How many aromatic R groups are there?

A

3

38
Q

How many basic R groups are there?

A

3

39
Q

How many acidic R groups are there?

A

2

40
Q

The pH at which the majority of molecules of a compound in solution have no net charge.

A

Isoelectric point

41
Q

If net charge is 0 or is neutral

A

Zwitterion

42
Q

If net charge is +1

A

Cationic Form

43
Q

If net charge is -1

A

Anionic Form

44
Q

T OR F:
The net charge on an amino acid depends on the pH of the solution in which it is dissolved.

A

True

45
Q

Who and in what year did he propose that proteins are long chains of amino acids joined by amide bonds?

A

Emil Fischer (1902)

46
Q

The special name given to the amide bond between three carboxyl group of one amino acid and the amino group of another.

A

Peptide Bond

47
Q

Usually found in trans conformation

A

Peptide Bond

48
Q

T OR F:
Peptide bonds has partial (60%) double bond character

A

False (40%)

49
Q

Peptide bonds are how long? It is shorter than a typical single bond but longer than a double bond

A

0.133 nm

50
Q

T or F:
The 6 atoms of the peptide bond group are always planar due to the double bond character.

A

True

51
Q

peptide bond (N)

A

Partially positive

52
Q

peptide bond (O)

A

partially negative

53
Q

Short polymers of amino acids

A

Polypeptides

54
Q

What do you call each unit of polypeptides?

A

Residue

55
Q

2 residues of polypeptides are called?

A

Dipeptide

56
Q

Oligopeptides have how many residues?

A

12-20 residues

57
Q

Tripeptides have how many residues?

A

3 residues

58
Q

T OR F:
Peptides are written from the left beginning with the three free -COO- group and ending with the -NH3+ on the right.

A

False (-NH3+ on left and -COO- on right)

59
Q

The amino acid at the end of the chain has the free -NH3+ group

A

N-terminal amino acid

60
Q

Has an almost equal number of acidic and basic side chains (pI is 6.8)

A

Hemoglobin

61
Q

PI is 4.9 and has more acidic side chains

A

Serum albumin

62
Q

T OR F:
Proteins are least soluble in water at their isoelectric points

A

True

63
Q

T OR F:
Proteins behave as zwitterions

A

True

64
Q

The sequence of amino acids in a polypeptide chain

A

Primary Structure

65
Q

Consists of two polypeptide chains having a total of 51 amino acids

A

Human Insulin

66
Q

T OR F:
Human insulin are connected by two interchain disulfide bonds

A

True

67
Q

Insulin consists of two polypeptide chains which are:

A

• A-chain
• B-chain

68
Q

A chain has how many residues?

A

21 residues

69
Q

B chain has how many residues?

A

30 residues

70
Q

Confirmation of amino acids in localized regions of a polypeptide chain. It can form wherever possible.

A

Secondary Structure

71
Q

What are the two common secondary structures?

A

• Alpha Helix
• Beta pleated Sheet

72
Q

A type of secondary structure in which two polypeptide chains align parallel to each other

A

B pleated sheets

73
Q

A type of secondary structure in which two polypeptide chain align parallel to each other

A

B pleated sheets

74
Q

A type of secondary structure in which a section of polypeptide chain coils into a spiral

A

Alpha Helix

75
Q

If all the R-groups on any one chain alternates from above to below the plane of the sheet, what is it called?

A

B Pleated sheet

76
Q

If all R groups point outward from the helix, what do you call it?

A

A Helix

77
Q

The three dimensional shape of the completed polypeptide

A

Tertiary Structure

78
Q

The arrangement of polypeptide chains into a noncovalenty bonded aggregation

A

Quaternary Structure

79
Q

Has 2 alpha chains of 141 amino acids each and 2 beta chains of 146 amino acids

A

Adult Hemoglobin

80
Q

Has 2 alpha chains and 2 gamma chains

A

Fetal hemoglobin

81
Q

What do you call it if the non-amino acid part of the protein is important to its function

A

Prosthetic group

82
Q

Who and when was the first who sequenced the two chains of insulin

A

Frederick Sanger (1953)

83
Q

Process of destroying the nativr conformation of a protein by chemical or physical means

A

Denaturation

84
Q

T OR F:
Heat can not disrupt hydrogen bonding

A

False (It can.)

85
Q

5 Denaturing agents:

A

• Heat
• 6 M aqueous urea
• Surface-active agents
• Reducing agents
• Heavy metal ions
• Alcohols

86
Q

5 Denaturing agents:

A

• Heat
• 6 M aqueous urea
•Surface-active agents
• Reducing agents
•Heavy metal ions

87
Q

An amino acid that cannot be synthesized de novo (since the beginning) by the organism and therefore must be supplied in the diet.

A

Essential Amino acid

88
Q

Its synthesis is innate in the body.

A

Non-essential amino acid

89
Q

Amino acids capable of yielding ketone bodies

A

Ketogenic Amino Acids

90
Q

Amino acids capable of yielding glucose

A

Glucogenic Amino acids