Chapter 21

Front 1

proteins are composed of multiple _____ bonds.

Back 1

amide

Front 2

Where is protein stored?

Back 2

casien

Front 3

______ tranport hemoglobin.

Back 3

proteins

Front 4

structure of protein

Back 4

collagen and keratin

Front 5

_____ is the catalyst of a protein that decreases activation energy.

Back 5

enzyme

Front 6

_____ is the amino acid that doesn't fit the formula of having an amino group and an acid group, but still has a chiral center

Back 6

proline

Front 7

Are amino acids arranged as D's or L's?

Back 7

L's

Front 8

Where are the C-terminus (carboxylic acid) and N-terminus (amine) located on amino acids?

Back 8

c- right
n- left

Front 9

With the exception of _____, all protein-derived amino acids have at least 1 stereocenter (the alpha-carbon) and are chiral

Back 9

glycine

Front 10

The majority of alpha amino acids have the ___-configuration at the alpha-carbon.

Back 10

L

Front 11

If an amino acid is non-polar, it contains ______ on the R group

Back 11

hydrocarbons

Front 12

If an amino acid is polar but has neutral side chains, it contains ____ on the R group.

Back 12

-OH or -SH

Front 13

If an amino acid is acidic, it contains a ____ on the R group.

Back 13

carboxylic acid

Front 14

If an amino acid is basic, it contains a ___ on the R group.

Back 14

amine

Front 15

All 20 amino acids are ___ amino acids meaning they contain a chiral C with R group attached.

Back 15

alpha

Front 16

For 19 of the 20 amino acids, the alpha amino group is primary, for ____, it is secondary.

Back 16

proline

Front 17

Except ____, the alpha carbon of each amino acid is a stereocenter.

Back 17

glycine

Front 18

2 amino acids that contain a second amino acid

Back 18

1) isoleucine
2) theonine

Front 19

____ is a compound where both a positive charge and a negative charge exist on the same molecule.

Back 19

Zwitterion

Front 20

AA are ____ compounds.

Back 20

ionic

Front 21

Ionic nature changes depending on solution ___.

Back 21

pH

Front 22

__ is the "isoelectric point" (ph where AA or protein has no charge)

Back 22

pl

Front 23

What is the charge of pl on AA?

Back 23

no charge

Front 24

If a zwitterion is more acidic, there is excess ___.

Back 24

H+

Front 25

If a zwitterion is more basic, there is excess ____.

Back 25

OH-

Front 26

The -SH group of cysteine is easily oxidized to a ____.

Back 26

disulfide

Front 27

_____ is a secondary structure in which a section of polypeptide coils. (slinky)

Back 27

alpha helix

Front 28

____ is a secondary structure in which 2 polypeptide chains align parallel/antiparallel to each other. (noodles)

Back 28

beta-pleated sheet

Front 29

____ is tough and insoluble protein in which the chain form long fibers or sheet.

Back 29

fibrous

Front 30

____ structure is responsible for the structure of fibrous protein.

Back 30

secondary

Front 31

____ are water soluble proteins whose chains are folded into compact, globular shape with hydrophilic groups on the outside.

Back 31

globular protein

Front 32

multiple secondary=

Back 32

tertiary

Front 33

_____ stabilizes the 3-D structure of tertiary structure.

Back 33

cross linking

Front 34

How are tertiary structures held together?

Back 34

h-bonds or disulfide bonds

Front 35

_____ is a protein composed of only amino acid residues.

Back 35

simple

Front 36

_____ is a protein htat incorporated 1 or more non-amino acid units in its structure.

Back 36

conjugated protein

Front 37

______ is the arrangement of polypeptide chains into a noncovalently bonded aggregation. (only attracted)

Back 37

quaternary structure

Front 38

triple helix is an ex. of ____ structure

Back 38

quaternary

Front 39

Fetal hemoglobin has a greater affinity for ____ than does adult hemoglobin.

Back 39

oxygen

Front 40

_____ is a glycosidic bond between the saccharide and the OH goup of serine, thronine, or hydroxylysine.

Back 40

O-linked saccharide

Front 41

____ is an N-glycosidic bond between the anomeric carbon of N-acetyl-D-glucosamine and the nitrogen of the side chain amide group of asparagine.

Back 41

N-linked saccharides

Front 42

_____ is the loss of secondary, tertiary, or quaternary protein structure due to disruption of non-covalent interactions and or disulfide bonds that leaves peptide bonds and primary structure intact.

Back 42

protein denaturation

Front 43

____ is a denaturation that breaks down protein in food.

Back 43

heat

Front 44

Salt is a denaturation that changes _____.

Back 44

pH

Front 45

___ is a denaturation that breaks disulfide bonds.

Back 45

reducing agent

Front 46

Tenderizor is an ex. of denaturation for ___

Back 46

agitation

Front 47

acid/base denaturation is an ex. of _____

Back 47

hydrolysis

Front 48

Enzymes decrease activation energy, do they change equilibrium?

Back 48

NO

Front 49

____ is an enzyme classification of the addition of groups to a double bond, or removal of groups to create a double bond.

Back 49

lyases

Front 50

____ is an enzyme classification of the joining of 2 molecules.

Back 50

ligases

Front 51

the majority of enzyme activity is at what temp?

Back 51

35-45

Front 52

What is the optimal pH for enzyme activity?

Back 52

6-7.5