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Biology > Proteins > Flashcards

Proteins Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What do proteins contain?

A

Carbon, hydrogen, oxygen and nitrogen

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2
Q

What monomers are proteins made up of?

A

Amino acids

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3
Q

What two other elements do some proteins contain?

A

Sulphur and phosphorus

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4
Q

How many amino acids are there that are commonly found in tissues and cells?

A

20

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5
Q

What is denaturing?

A

The permanent loss of specific 3D shape of a protein molecule

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6
Q

What 4 components make up the structure of an amino acid?

A

R group, amino group, carboxyl group and hydrogen

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7
Q

What group in amino acids is variable?

A

R group

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8
Q

What does Zwitterion mean?

A

Amino acids can be both positive and negative charged as they have acid and base properties

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9
Q

How do peptide bonds form?

A

Condensation reaction between 2 amino acids

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10
Q

What two groups does a peptide bond form between?

A

Carboxyl and amino group

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11
Q

How do you test for proteins?

A

Add sodium hydroxide and very dilute copper II sulfate and mix gently

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12
Q

What colour change indicates a protein is present?

A

Blue to purple due to the presence of peptide bonds

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13
Q

What four structures are there of proteins?

A

Primary, secondary, tertiary and quaternary

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14
Q

What two things does the order and sequence of amino acids determine?

A

Shape and function

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15
Q

What is the primary structure of a protein?

A

Sequence of amino acids found in a polypeptide chain

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16
Q

What bonds are found in the primary structure?

A

Peptide bonds

17
Q

What is the secondary structure of a protein?

A

Polypeptide bonds form an alpha helix shape due to hydrogen bonding although pleated sheets can also occur

18
Q

What bonds occur in the secondary structure?

A

Peptide and hydrogen bonds

19
Q

What is the tertiary structure of a protein?

A

Bending and twisting of the polypeptide helix into a compact structure

20
Q

What bonds are there in the tertiary structure?

A

Peptide, hydrogen, ionic and disulphide bonds

21
Q

What is the quaternary structure of a protein?

A

Combination of a number of different polypeptide chains into a large 3D shape

22
Q

What bonds are found in the quaternary structure?

A

Peptide, hydrogen, ionic and disulphide bonds

23
Q

What effect does temperature have on proteins?

A

Breaks the hydrogen bonds destroying the 3D structure and denaturing the protein

24
Q

What effect does alcohol have on proteins?

A

Break the hydrogen bonds and alters the hydrophobic interactions ruining the 3D shape and denaturing the protein

25
Q

What is the effect of acid on a protein?

A

Hydrogen and ionic bonds break unravelling the structure so the inside parts of the structure are exposed to dorm bonds with other protein molecules that stick together and become insoluble.

26
Q

What are the two typed of proteins?

A

Globular and fibrous proteins

27
Q

What is an example of a globular protein?

A

Enzymes and haemoglobin

28
Q

What is an example of a fibrous protein?

A

Collagen

29
Q

What is the difference in function between a globular and fibrous protein?

A

Globular have metabolic functions

Fibrous have structural functions

30
Q

What is the structure of a fibrous protein?

A

Form long chains that are parallel they are linked by cross bridges to form very stable molecules

31
Q

What type of structure does collagen have?

A

Rope like

32
Q

How is collagen prevented from being weak at one point?

A

The points where the molecules start and end are spread throughout

33
Q

Where is collagen found?

A

In tendons

34
Q

Why is collagens structure good for its function?

A

It has long rope like chains which are strong but can also be stretched when a muscle contracts

35
Q

How does cross linkages increase the stability and strength of collagen?

A

Prevent the polypeptide chains from sliding past each other instead they work as one large molecule

Biology (22 decks)

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