Module 2 Section 2 - Proteins Flashcards

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1
Q

What are proteins

A

Polymers

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2
Q

What are amino acids

A

Monomers

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3
Q

A dipeptide is …..

A

Formed when TWO amino acids join together

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4
Q

A Polypeptide is…..

A

Formed when MORE THAN TWO amino acids are joined together

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5
Q

All amino acids have….

A

The same general structure. A carboxyl group and amino group

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6
Q

What is the difference between amino acids

A

The variable group they contain

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7
Q

What elements doall amino acids contain

A

Carbon
Oxygen
Hydrogen
Nitrogen

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8
Q

What do some amino acids contain

A

Sulfur (alongside C,H,O,N)

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9
Q

What are amino acids linked by

A

Peptide bonds

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10
Q

Amino acids and peptide bonds form to make

A

Dipeptides and polypeptides

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11
Q

What is released during the reaction when amino acids are joined together

A

A molecule of water - condensation reaction

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12
Q

The reverse reaction of when peptide bonds between amino acids breaks does what

A

Adds a molecule of water - hydrolysis reaction

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13
Q

What are the four structural levels of protein

A

Primary
Secondary
Tertiary
Quaternary

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14
Q

What is the primary structure of a protein

A

The sequence of the amino acids in the polypeptide chains

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15
Q

What is the secondary structure

A

hydrogen bonds form between amino acids in the chain. This automatically coils into an alpha helix or fold into a beta pleated sheet

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16
Q

What is tertiary structure

A

The coiled or folded chain of amino acids is often coiled and folded further. For proteins made from a single polypeptide chain the tertiary formed their final 3D structure

17
Q

What is quaternary structure

A

Some proteins are made from several polypeptide chains held together by bonds. For proteins made from more than one polypeptide chain, the quaternary is the protein final 3D structure

18
Q

What is the primary structure held together by

A

Peptide bonds between the amino acids

19
Q

Secondary structures are held together by…..

A

Hydrogen bonds

20
Q

Tertiary bonds are held together by

A

Ionic bonds
Disulphide bonds
Hydrophobic or hydrophilic interactions
Hydrogen bonds

21
Q

In tertiary structure ionic bonds are used to hold it together, what does this mean

A

These are attractions between negatively charged R-groups and positively charged R-groups on different parts of the molecule

22
Q

In tertiary structure disulphide bonds are used to hold it together, what does this mean

A

Whenever two molecules of the amino acid cysteine come close together, the sulfur atoms in one cysteine, bonds to the sulfur in the other cysteine forming a disulphide bond

23
Q

In tertiary structure a hydrophobic and hydrophilic interactions holds the structure together. What does this mean

A

When hydrophobic r groups are close together in the protein, they tend to clump together. This means that hydrophilic r-groups are more likely to be pushed to the outside, which affects how the protein folds up into final structure.

24
Q

In tertiary structure, hydrogen bonds are used to hold up the structure, what does this mean

A

Weak bonds form between slightly positively charged hydrogen atoms in some r groups and slightly negative charged atoms in other r groups on the polypeptide chain.

25
Q

A quarternary structure is held together by

A

tends to be determined by the tertiary structure of the individual polypeptide chains being bonded together. can be influenced by all the bonds mentioned e.g. ionic, disulphide, hydrophobic and hydrophilic interactions and hydrogen bonds

26
Q

In a globular protein what tends to be pushed on the outside of the molecule

A

The hydrophilic r-groups

27
Q

What causes the globular protein to push the hydrophilic r-group on the amino acids to the outside of the molecule

A

The hydrophobic and hydrophilic interactions in the tertiary structure

28
Q

are globular protein soluble

A

yes meaning they are easily transported in fluids

29
Q

examples of globular proteins are

A

haemoglobin
insulin
amylase

30
Q

what are the properties of a fibrous protein

A

-insoluble
-strong
-fairly unreactive

31
Q

what are the example of fibrous proteins that we need to know

A

collagen
keratin
elastin

32
Q

where is collagen found

A

animal connective tissues (bone, skin, muscle etc.)

33
Q

what can bind to the protein to increase rigidity

A

minerals

34
Q

where is keratin found

A

in many external structures of animals, such as skin, hair, nails etc.

35
Q

keratin can either be

A

-flexible (as it is in skin)
-hard and tough (as it is in nails)

36
Q

where is elastin found

A

in connective tissue, such as skin, blood vessels, and some ligament

37
Q

a change in one amino acids in the primary structure means what

A

a change in one amino acid may change the structure of the whole protein

38
Q

different protein have….

A

different sequences of amino acids in their primary structure