Chapter 3

Question 1

What do amino acids contain?

Answer 1

Carboxy,l Amino, and a hydrogen group

Question 2

What is the way to differentiate the 20 different amino acids?

Answer 2

the difference is in their side chains

Question 3

Of the amino acid groups which portion of the structure takes a negative charge?

Answer 3

carboxyl group

Question 4

What happens when an amino acid is exposed to an aqueous environment?

Answer 4

it gains a proton and takes a positive charge.

Question 5

What is the largest group of amino acids? (reference to the 20 different kinds)

Answer 5

non polar side chain group

Question 6

what makes an amino acid polar?

Answer 6

the covalent bonds on the peripheral side allow them to make hydrogen bonds.

Question 7

Are amino acids bases or acids and strong or weak?

Answer 7

weak acids and bases
basic- if the side chain picks up a proton
acidic- if it contains a carboxyl side chain

Question 8

What is important of the amino acids side chains?

Answer 8

The properties of their side chain dictate how reactive and soluble they are

Question 9

How is it easy to get amino acids in the prebiotic earth?

Answer 9

carbon + heat + pressure

Question 10

What describes the fact that 19/20 amino acids can be found in two ways?

Answer 10

optical isomers, basically asymetry

Question 11

What is the only amino acid that has one form

Answer 11

Glycine

Question 12

What way do organisms absorb amino acids (which form)

Answer 12

left handed

Question 13

What are peptide bonds?

Answer 13

covalent bonds that link amino acids together

Question 14

What does the vastly differing shapes of proteins have to do with?

Answer 14

The greater the diversity of shape and structure the vastly differing things it can do in terms of function

Question 15

What are the terminuses of amino acids?

Answer 15

N and C.

Question 16

Which end do you begin numbering the amino acids?

Answer 16

the N terminus

Question 17

Describe the primary sequence of protein folding?

Answer 17

the linear structure of amino acids is altered for further folding and is stabilized via peptide bonds

Question 18

Describe the secondary sequence of protein folding?

Answer 18

the secondary structures are stabilized, while an oxygen and a hydrogen on both ends form hydrogen bond, thus folding the shape.

Question 19

Describe the tertiary sequence of protein folding?

Answer 19

there is a stabilized shape, resulting from hydrogen bonds, ionic, disulfide bond, van der waals interactions, and other stabilizing forces that form a very diverse and independent structure. The R groups is what is bonded in tis instance.

Question 20

Describe the quaternary sequence of protein folding?

Answer 20

when two different polypeptides come together to make the final protein

Question 21

What is protein denaturation?

Answer 21

when the protein unfolds via chemicals in the environment

Question 22

Intrinsic factors:

Answer 22

inability for polar molecules to form hydrogen bonds

Question 23

extrinsic factors:

Answer 23

chaperons and chaperonins

Question 24

What are chapernoes and chaperonins?

Answer 24

chaperons: grab onto unfolded proteins
chaperonins: create a small barrel structure to enclose and randomize/complexify the protein .