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Proteins Flashcards

1
Q

How are proteins connected?

A

Through the chemical and physical activities of the cell

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2
Q

What are the different forms that proteins function as?

A

Enzymes, hormones, antibodies, oxygen transporters,

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3
Q

What do proteins form?

A

majority of the skin, hair, feathers, nails, and cartilage

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4
Q

basics of proteins?

A

3d molecules, building blocks of amino acids

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5
Q

properties of amino acids

A

> grouped by polarity
variable R groups (side chains) confer different properties to each amino acid
polar, water soluble
non polar, water insoluble
positively charged
negatively charged

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6
Q

How many proteinogenic amino acids build humans?

A

20

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7
Q

Where are non essential amino acids made?

A

in the body

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8
Q

where do essential amino acids come from?

A

eaten in our diet

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9
Q

What is polymerisation?

A

When many amino acid monomers can be joined together through a series of condensation reactions

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10
Q

what is a polypeptide?

A

Formed from the condensation of many amino acids

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10
Q

What bond are the amino acids binded by in a protein?

A

Peptide bond

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10
Q

What are amino acids?

A

The monomers that bind together to form polymers called polypeptides (proteins)

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11
Q

What group is NH2 in an amino acid?

A

The amine group

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11
Q

what group is COOH in an amino acid?

A

the carboxyl group

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11
Q

What group is H in an amino acid?

A

A hydrogen atom

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12
Q

What group is R in an amino acid?

A

the side group

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13
Q

Is the R group the same across all amino acids?

A

No they are different in each amino acid

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14
Q

What does the R group determine in an amino acid?

A

How the amino acid interacts and bonds with other amino acids in the polypeptide

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15
Q

What is the central carbon in an amino acid?

A

The control/ alpha carbon

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16
Q

How many different amino acids are common in all organisms?

A

20

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17
Q

What does glycine have in its R group?

A

A hydrogen atom. It is the only amino acid that does not have carbon in its R group

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18
Q

What are polypeptides made from?

A

Chains of amino acids

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19
Q

What are end terminals of polypeptides?

A

Amino acids at the end of each polypeptide chain.

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20
Q

What is the N terminal

A

amine terminal

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21
What is the C terminal
the carboxyl terminal
22
What parts of the amino acids bind together forming a peptide bond?
The carboxyl group of the first amino acid and the amine group of the second amino acid.
23
What molecule is released as a by product of the peptide bond?
A single water molecule
24
What type of bond is a peptide bond?
A covalent bond
25
Functions of proteins- antibodies
- Made up of polypeptide chains - Used in immune response - Antibodies are diverse proteins - Each antibody has a different series of amino acids
26
Does each antibody have the same series of amino acids?
No- Each antibody has a different series of amino acids
27
What are diverse proteins?
Antibodies
28
What do transport proteins/ channel proteins do?
They transport molecules across the cell membrane, as well as transporting molecules that are too large to diffuse freely or molecules that carry charge
29
What are enzymes?
Biological catalysts
30
How are most enzymes structured?
They are tightly folded, complex proteins that are soluble and help increase the rate of reaction
31
What are structural proteins?
Long, strong polypeptide chains
32
How are structural proteins connected?
They are connected by cross links that hold the chains parallel to eachother
33
What are examples of structural proteins?
Collagen and Keratin
34
What determines the primary structure of a protein?
The order of amino acids, and the gene encoding of the protein
35
What happens if there is a change in the nucleotide sequence of the genes coding region?
Possibly a different amino acid being added to the growing polypeptide chain which could change the proteins structure and function.
36
What forms the secondary structure of a protein?
Folding between amino acids in the polypeptide chain, as well as hydrogen bonds
37
How are hydrogen bonds involved in the secondary structure of a protein?
Amino acids form hydrogen bonds between other amino acids in the chain. This causes the protein to fold into specific structures, and the folding of the polypeptide determines the secondary structure
38
What are common secondary structures of proteins?
Alpha helix, and beta pleated sheets
39
What is an example of an alpha helix structure?
Rhodopsin (pigment in the eyes)
40
What is an example of the beta pleated sheets structure?
Silk
41
Is the secondary structure of a protein stable?
Yes as individual hydrogen bonds are weak however there are many bonds across the molecule, leading to high stability of the protein.
42
What can weaken the hydrogen bonds in the secondary structure of a protein?
Environmental factors such as temperature or pH
43
What is the tertiary structure of a protein?
The secondary polypeptide folds further to form a tertiary three dimensional polypeptide chain
44
How are the R groups of amino acids relevant to the tertiary structure of a protein?
Interactions between R groups create the complex 3d tertiary structure of proteins.
45
what is the 3d tertiary structure?
It is usually coiled or folded
46
What happens when a protein loses its 3d shape?
It may no longer be able to function
47
What interactions are there that determine the final 3d shape of a protein?
Weak and strong interactions- ionic bonds, hydrogen bonds, and disulfide bridges
48
49
What does the buiret test detect?
Peptide bonds, showing that a protein is present
50
what three aspects are there of the induced fit model?
1 The enzyme- substrate molecule 2 The enzymes substrate complex (when the substrate binds to the active site. 3 enzyme + product molecule (when the products are released from the enzyme
51
Are ionic bonds between amino acids common?
No they are quite rare
52
How do amino acids make ionic bonds?
Charged amino acids have a positively or negatively charged ion in their side chain(R group). Charged amino acids can form relatively strong ionic bonds with other charged amino acids
53
What are disulfide bridges also known as?
s-s bonds or disulfide bonds
54
What are disulfide bridges?
Covalent bonds within proteins containing cyteine (CYS) amino acids
55
What are the features of hydrogen bonds in amino acids?
They are relatively weak individually but when there are many of them, the overall stability of the tertiary structure increases
56
What is the quarternary structure of proteins?
Multiple 3d polypeptides joined together in one protein
57
Summary of the primary structure
A sequence of amino acids
58
Summary of secondary structure
Folding between amino acids in the polypeptide chain, with hydrogen bonds
59
Summary of tertiary structure
3D structure made up of ionic bonds, hydrogen bonds, and disulfide bridges.
60
Summary of quarternary structure
multiple polypeptides joined in one protein
61
What factors determine proteins conformation?
-Occurs during protein synthesis within cells. -Depends on physical conditions of the environment (pH, temp, salinity etc)
62
What can change in environment lead to?
Denaturation of a protein, and a denatured protein is biologically inactive. However it can renature if primary structure is not lost.

Biological molecules (9 decks)

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