Proteins

Question 1

the functional groups

Answer 1

amine group and carboxyl group

Question 2

how many amino acids in a protein

Answer 2

20

Question 3

what is L vs D

Answer 3

L/levo: amine group on the left;

D/dextro: amine group on the right

Question 4

what is a peptide bond; what type

Answer 4

amine group to carboxyl; covalent

Question 5

what is the first amino acid of all proteins

Answer 5

aug

Question 6

monomers of proteins

Answer 6

amino acid

Question 7

when you digest proteins what process breaks them down into amino acids

Answer 7

hydrolysis

Question 8

2 amino acid

Answer 8

dipeptide

Question 9

oligopeptide

Answer 9

3-10 amino acids

Question 10

more than 10 amino acid

Answer 10

polypeptide

Question 11

the type of most proteins (# of amino acids) and how many they typically have

Answer 11

polypeptide; 350

Question 12

how many essential AA

Answer 12

10

Question 13

how many nonessential AA

Answer 13

10

Question 14

how do we get essential AA

Answer 14

must be eaten

Question 15

how do we get nonessential AA

Answer 15

we make them

Question 16

how many proteins in a cell and how long they last

Answer 16

1 billion; about a week (we are constantly making them)

Question 17

what are the 4 types of R groups

Answer 17

basic, acidic, polar, nonpolar

Question 18

name the basic R groups

Answer 18

lysine, arginine, histidine

Question 19

what makes an R group basic

Answer 19

positive charge

Question 20

how to help recognize a basic R group

Answer 20

NH

Question 21

name the acidic R groups

Answer 21

aspartic acid, glutamic acid

Question 22

what makes an R group acidic

Answer 22

neg charge (donate protons)

Question 23

how to recognize an acidic r group

Answer 23

C double bonded to O and bonded to O

Question 24

how to recognize an uncharged polar R group

Answer 24

OH

Question 25

charge of polar R groups

Answer 25

neutral

Question 26

how to help recognize a nonpolar R group

Answer 26

CH

Question 27

charge of nonpolar R group

Answer 27

neutral

Question 28

what allows for the "mirror image" isomers

Answer 28

the alpha carbon is asymmetric

Question 29

types of protein functions: enzyme

Answer 29

speeds up chemical reaction (by catalyzing covalent bond breakage or formation)

Question 30

types of protein functions: structural protein

Answer 30

holds up (provides mechanical support)

Question 31

types of protein functions: transport protein

Answer 31

carries small molecules or carbons; | example: hemoglobin carries oxygen

Question 32

types of protein functions: motor protein

Answer 32

slide filaments (generates movement)

Question 33

types of protein functions: storage protein

Answer 33

stores small molecules

Question 34

signal protein

Answer 34

tells cells to ______ (carries signals between cells)

Question 35

types of protein functions: receptor proteins

Answer 35

detects signals (and transmits them)

Question 36

types of protein functions: gene regulatory protein

Answer 36

switch genes on/off (p53)

Question 37

types of protein functions: special purpose proteins

Answer 37

varied

Question 38

how many AA commonly found in proteins

Answer 38

20

Question 39

what process do AA bond

Answer 39

dehydration synthesis

Question 40

what causes proteins to fold; and what is it based on

Answer 40

R groups; charge

Question 41

what form are most proteins in

Answer 41

globular (folded)

Question 42

what decided the shape of a protein

Answer 42

AA sequence

Question 43

what are the four noncovalent forces found in protein folding

Answer 43

ionic bonding, hydrogen bonding, VanDer Wahls forces, hydrophobic interactions

Question 44

ionic bonding

Answer 44

positive to negative

Question 45

hydrogen bonding

Answer 45

positive hydrogen to negative oxygen

Question 46

VanDer Wahls forces

Answer 46

atoms forced close to each other (weak)

Question 47

hydrophobic interactions

Answer 47

they turn in to avoid water

Question 48

what is the primary level of protein structure

Answer 48

amino acid sequence (always!)

Question 49

what is the secondary level of protein structure

Answer 49

common folding patterns

Question 50

what are the common folding patterns in the secondary level or protein structure

Answer 50

1. alpha helix- "slinky" | 2. beta sheet- "elongated slinky"

Question 51

what is the tertiary level of protein structure

Answer 51

3-D shape (final)

Question 52

what is the quarternary level of protein structure

Answer 52

more than 1 polypeptide (1 protein, multiple polypeptides)

Question 53

conformation

Answer 53

overall, final 3-D shape (use x-ray diffraction)

Question 54

native protein

Answer 54

normal, natural state

Question 55

denatured

Answer 55

lost its shape

Question 56

what are the 2 factors that can denature a protein

Answer 56

temperature, pH-isoelectric point

Question 57

why does temp denature

Answer 57

hotter, breaks weak bonds, changes shape

Question 58

isoelectric point

Answer 58

pH at which a protein becomes neutral

Question 59

negative has _____ isoelectric points

Answer 59

low

Question 60

positive have _____ isoelectric points

Answer 60

high

Question 61

components of enzymes

Answer 61

- most* are proteins (*rna) - shape is important - specific - not changed, used repeatedly

Question 62

enzyme equation

Answer 62

E+S–>ES(noncovalent bond here)–>EP–>E+P

Question 63

what are E, S, and P

Answer 63

Enzyme, substrate, product

Question 64

what happens to the substrate

Answer 64

it is altered permanently (into the product)

Question 65

what enzyme would digest a fat

Answer 65

lipase

Question 66

at high temps the rate of enzyme action decreases because

Answer 66

the increased heat alters the site of the active enzyme

Question 67

enzymes influence chemical reactions in living systems by

Answer 67

affecting the rate at which reactions occur

Question 68

which group of organic compounds includes enzymes

Answer 68

proteins

Question 69

what does the lock and key hypothesis attempt to explain

Answer 69

mechanism of enzyme specificity

Question 70

a substance acted upon by an enzyme

Answer 70

substrate

Question 71

enzymes are

Answer 71

specific

Question 72

at 0°C most enzymes are

Answer 72

inactive

Question 73

what enzyme is in maltase but not maltose

Answer 73

nitrogen

Question 74

what is an environmental condition that has the LEAST effect on the rate of enzyme controlled reactions

Answer 74

light present

Question 75

lipase, maltase, and protease are examples of

Answer 75

enzymes