PROTEINS Flashcards

(90 cards)

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
A compound that contains both an amino group and a carboxyl group
Amino acid
26
Building blocks of proteins
Amino acid
27
How many primordial amino acids are there?
20
28
T OR F: All amino acids are in the a-L configuration
True
29
How many standard amino acids contain a chiral center?
19/20
30
The COOH is put at the top
Fischer Projection
31
Positioning NH2 on the left
L-Isomer
32
Positioning NH2 on the right
D-Isomer
33
T OR F: When not in pure form, amino acids are white crystalline solids.
False (Pure form.)
34
What are incorporated into polypeptides during protein synthesis?
20 Primordial amino acids
35
How many aliphatic R groups are there?
7
36
How many polar R groups are there?
5
37
How many aromatic R groups are there?
3
38
How many basic R groups are there?
3
39
How many acidic R groups are there?
2
40
The pH at which the majority of molecules of a compound in solution have no net charge.
Isoelectric point
41
If net charge is 0 or is neutral
Zwitterion
42
If net charge is +1
Cationic Form
43
If net charge is -1
Anionic Form
44
T OR F: The net charge on an amino acid depends on the pH of the solution in which it is dissolved.
True
45
Who and in what year did he propose that proteins are long chains of amino acids joined by amide bonds?
Emil Fischer (1902)
46
The special name given to the amide bond between three carboxyl group of one amino acid and the amino group of another.
Peptide Bond
47
Usually found in trans conformation
Peptide Bond
48
T OR F: Peptide bonds has partial (60%) double bond character
False (40%)
49
Peptide bonds are how long? It is shorter than a typical single bond but longer than a double bond
0.133 nm
50
T or F: The 6 atoms of the peptide bond group are always planar due to the double bond character.
True
51
peptide bond (N)
Partially positive
52
peptide bond (O)
partially negative
53
Short polymers of amino acids
Polypeptides
54
What do you call each unit of polypeptides?
Residue
55
2 residues of polypeptides are called?
Dipeptide
56
Oligopeptides have how many residues?
12-20 residues
57
Tripeptides have how many residues?
3 residues
58
T OR F: Peptides are written from the left beginning with the three free -COO- group and ending with the -NH3+ on the right.
False (-NH3+ on left and -COO- on right)
59
The amino acid at the end of the chain has the free -NH3+ group
N-terminal amino acid
60
Has an almost equal number of acidic and basic side chains (pI is 6.8)
Hemoglobin
61
PI is 4.9 and has more acidic side chains
Serum albumin
62
T OR F: Proteins are least soluble in water at their isoelectric points
True
63
T OR F: Proteins behave as zwitterions
True
64
The sequence of amino acids in a polypeptide chain
Primary Structure
65
Consists of two polypeptide chains having a total of 51 amino acids
Human Insulin
66
T OR F: Human insulin are connected by two interchain disulfide bonds
True
67
Insulin consists of two polypeptide chains which are:
• A-chain • B-chain
68
A chain has how many residues?
21 residues
69
B chain has how many residues?
30 residues
70
Confirmation of amino acids in localized regions of a polypeptide chain. It can form wherever possible.
Secondary Structure
71
What are the two common secondary structures?
• Alpha Helix • Beta pleated Sheet
72
A type of secondary structure in which two polypeptide chains align parallel to each other
B pleated sheets
73
A type of secondary structure in which two polypeptide chain align parallel to each other
B pleated sheets
74
A type of secondary structure in which a section of polypeptide chain coils into a spiral
Alpha Helix
75
If all the R-groups on any one chain alternates from above to below the plane of the sheet, what is it called?
B Pleated sheet
76
If all R groups point outward from the helix, what do you call it?
A Helix
77
The three dimensional shape of the completed polypeptide
Tertiary Structure
78
The arrangement of polypeptide chains into a noncovalenty bonded aggregation
Quaternary Structure
79
Has 2 alpha chains of 141 amino acids each and 2 beta chains of 146 amino acids
Adult Hemoglobin
80
Has 2 alpha chains and 2 gamma chains
Fetal hemoglobin
81
What do you call it if the non-amino acid part of the protein is important to its function
Prosthetic group
82
Who and when was the first who sequenced the two chains of insulin
Frederick Sanger (1953)
83
Process of destroying the nativr conformation of a protein by chemical or physical means
Denaturation
84
T OR F: Heat can not disrupt hydrogen bonding
False (It can.)
85
5 Denaturing agents:
• Heat • 6 M aqueous urea • Surface-active agents • Reducing agents • Heavy metal ions • Alcohols
86
5 Denaturing agents:
• Heat • 6 M aqueous urea •Surface-active agents • Reducing agents •Heavy metal ions
87
An amino acid that cannot be synthesized de novo (since the beginning) by the organism and therefore must be supplied in the diet.
Essential Amino acid
88
Its synthesis is innate in the body.
Non-essential amino acid
89
Amino acids capable of yielding ketone bodies
Ketogenic Amino Acids
90
Amino acids capable of yielding glucose
Glucogenic Amino acids