Module 4.3 Proteins

Question 1

Proteins are the most abundant of all the

Answer 1

biomolecules

Question 2

Proteins are essential for all

Answer 2

living organisms including bacteria, plants and animals.​

Question 3

What shapes can proteins have?

Answer 3

Proteins can be globular, tubular, or stringy, among other wide variety of shapes.

Question 4

List some functions of proteins.

Answer 4

• Enzymes
• Hair
• Muscle fibers
• Hormones
• Antibodies

Question 5

Amino acids are

Answer 5

monomers are protein

Question 6

What are the monomers of proteins?

Answer 6

Amino acids are the monomers of proteins.

Question 7

How many different amino acids are there?

Answer 7

There are 20 different amino acids.

Question 8

Each amino acid is given a

Answer 8

3 letter designation

Question 9

What is the three-letter designation for serine?

Answer 9

Ser

Question 10

What is the three-letter designation for methionine?

Answer 10

Met

Question 11

What is the three-letter designation for alanine?

Answer 11

Ala

Question 12

Amino acid naming typically end in

Answer 12

-ine

Question 13

Define essential amino acids.

Answer 13

Essential amino acids are those humans need in their diet. We can’t make these ourselves.

Question 14

Define non-essential amino acids.

Answer 14

Non-essential amino acids are those humans can make in their cells.

Question 15

What groups do all amino acids have?

Answer 15

• Amino group
• Carboxyl group
• R (variable) group
• Hydrogen

Question 16

Amino Acid Structure

Answer 16

Question 17

Amino Acids always have a

Answer 17

Central Carbon with a Hydrogen attached to it. It will also have an amino group (n) and a carboxyl groups (double bonded 0)

Question 18

What is always different in an amino acid structure?

Answer 18

The R group. It can be extra carbons, ring structures, just about anything. This is the difference when it comes to functionality

Question 19

What happens to amino acids in solution?

Answer 19

The acidic carboxyl group donates its H+ to the basic amino group, resulting in a positively charged amino end and a negatively charged carboxyl end.

Question 20

What is the R group of an amino acid?

Answer 20

The R group is variable and differs from one amino acid to another.

Question 21

List the four types of R groups in amino acids.

Answer 21

• Non-polar and hydrophobic
• Polar and hydrophilic
• Acidic and hydrophilic
• Basic and hydrophilic

Question 22

Acidic and basic amino acids are

Answer 22

ionic and charged in solutions

Question 23

Amino acids are linked by the

Answer 23

dehydration reaction

Question 24

What is a peptide bond?

Answer 24

A peptide bond is the covalent bond that forms between amino acids after/during? a dehydration reaction

Question 25

What is a dipeptide?

Answer 25

A dipeptide is 2 amino acids connected by a peptide bond.

Question 26

What is a peptide?

Answer 26

A peptide is made up of less than 50 amino acids.

Question 27

What is a polypeptide?

Answer 27

A polypeptide is larger than 50 amino acids and is called a protein when it folds.

Question 28

Once a peptide or polypeptide folds, it is called a

Answer 28

protein

Question 29

If proteins loose it's shape or structure, it can loose it's

Answer 29

functionality

Question 30

What is the hydrolysis reaction in the context of digestion of proteins in our stomach?

Answer 30

The hydrolysis reaction is used to break down proteins into its amino acids.

Question 31

What determines the function of a protein?

Answer 31

The structure of the protein determines its function.

Question 32

The long chain of amino acids, the polypeptide, is like a ribbon and begins to fold into its

Answer 32

characteristic shape that will determine the structure of the protein

Question 33

Protein misfolding can create

Answer 33

problems

Question 34

What are the four levels of protein structure?

Answer 34

* Primary * Secondary * Tertiary * Quaternary

Question 35

What characterizes primary protein structure?

Answer 35

The sequence of amino acids held together by covalent bonds. Looks like a necklace

Question 36

What characterizes secondary protein structure?

Answer 36

Folding of part of primary structure into curly-hue (alpha helix) or zigzag (beta pleated sheets) held together by weak hydrogen bonds.

Question 37

What characterizes tertiary protein structure?

Answer 37

Folding of polypeptide into its 3D shape held together by interactions of R groups.

Question 38

What characterizes quaternary protein structure?

Answer 38

Interaction between 2 or more polypeptides held together with bonds of the backbone and R groups.

Question 39

What percentage of our protein is made from 3 polypeptides in a triple helix​?

Answer 39

40% of our protein is made from 3 polypeptides in a triple helix​

Question 40

The misfolding of proteins often occurs when

Answer 40

the wrong amino acid is inserted into the primary structure​

Question 41

What diseases are associated with misfolded proteins?

Answer 41

Diseases such as Alzheimer’s and Parkinson’s are associated with misfolded proteins.

Question 42

What is denaturation?

Answer 42

Denaturation is when the shape of a protein is destroyed, thus destroying its function.

Question 43

What factors can denature proteins?

Answer 43

* Temperature * pH * Salt concentration

Question 44

What happens to egg white proteins when cooked?

Answer 44

Heating denatures the proteins, turning them from clear to white.

Question 45

How does pH affect proteins?

Answer 45

Acidic or basic environments can denature proteins.

Question 46

What is the space-filling model of proteins?

Answer 46

It shows atoms that make up the protein.

Question 47

What does the ribbon model of proteins illustrate?

Answer 47

It shows alpha helix structures and beta pleated sheets.

Question 48

What does the 3-D ('Blob') model of proteins show?

Answer 48

It shows the overall shape of a protein and its polypeptides.