3.5: Proteins include a diversity of structures, resulting in a wide range of functions

Question 1

What is the structure of an amino acid ?

Answer 1

In amino acids, there is a central carbon, amino on the left and carboxyl on right. hydrogen on the bottom and R group on the top

Question 2

What is represented by R? How many are there?

Answer 2

The R group represents the various side chains that can be hydrophobic,philic, acidic, or basic. There are 20

Question 3

Why are some R groups hydrophobic, philic, acidic, or basic.

Answer 3

hydrophobic: tons of hydrocarbons, nonpolar
hydrophilic: there are carbonyl, hydroxyl, and sulfhydrl groups
acidic: - charges mainly in oxygen
basic: + charges mainly NH .

Question 4

peptide bond

Answer 4

bond between the hydroxyl and carboxyl group of 2 amino acids . dehydration synethesis

Question 5

polypeptide

Answer 5

many amino acids bonded to each other in chain

Question 6

Primary level of protein structure, give an example

Answer 6

the primary level is where the polypeptide cain is formed with no folding or coiling yet. An example of this would be transthyretin which is made of 4 polypeptide chains each containign 127 amino acids.

Question 7

secondary level of protein structure, give an example

Answer 7

the secondary level is where the polypeptide chain starts to fold into a alpha helix, coild sturcture, and a beta pleated sheat,folds over each other. This happends due to hydrogen bonding between back bones. Example: transthyretin

Question 8

tertiary level of protein structure, give an example

Answer 8

in the tertiary level, the polypeptide chain continues to fold and becomes a gloubular protein or an enzyme.

Question 9

explain the interactions that take place in the folding of the polypeptide in the tertiary level

Answer 9

between R groups
hydrophobic interactions: the hydrophobic groups are forced into close association due to water on the outside

van der waals: weak interactions between atoms

Disulfide brideges: bond between 2 sulfide atoms/ sulf hydryl groups.

h bonds: between hydgrogens and oxygens

ionic bonds: between acids and bases

Question 10

Define denaturation, and give at least three ways a protein may become denatured.

Answer 10

when a protein unravels or loses shape

1. other denatured proteins
2. temp chanegs
3. pH changes

Question 11

chaperonin proteins

Answer 11

they assist the folding of other proteins, they isolate them from the surrounding environment.

Question 12

Quatenary Structure

Answer 12

when 2 or more polypeptide chains combine, they form a bigger protein.They are made with the same interactions as tertiary.

Question 13

sickle cell disease

Answer 13

when the hemoglobin blood cells start to deform and make sickle shapes , this can stop blood flow over time.

Question 14

Define Enyme Protein and give example

Answer 14

accelerates reactions, digestive enzymes can break down food with hydrolysis

Question 15

Define storage Protein and give example

Answer 15

stores amino acids, casein found in milk provides body with amino acids

Question 16

Define defensive Protein and give example

Answer 16

protects against disease, antibodies destroy viruses and bacteria

Question 17

Define transport Protein and give example

Answer 17

transports nutrients, hemoglobin transports O2 from lungs to the rest of the body

Question 18

Define receptor Protein and give example

Answer 18

can recept sginals from other nuerons, receptor proteins are a good example of this