Print Options

Card layout: ?

← Back to notecard set|Easy Notecards home page

Instructions for Side by Side Printing
  1. Print the notecards
  2. Fold each page in half along the solid vertical line
  3. Cut out the notecards by cutting along each horizontal dotted line
  4. Optional: Glue, tape or staple the ends of each notecard together
  1. Verify Front of pages is selected for Viewing and print the front of the notecards
  2. Select Back of pages for Viewing and print the back of the notecards
    NOTE: Since the back of the pages are printed in reverse order (last page is printed first), keep the pages in the same order as they were after Step 1. Also, be sure to feed the pages in the same direction as you did in Step 1.
  3. Cut out the notecards by cutting along each horizontal and vertical dotted line
To print: Ctrl+PPrint as a list

75 notecards = 19 pages (4 cards per page)

Viewing:

Chapter 16

front 1

classify protein according to its function:
hemoglobin, oxygen carrier in the blood

back 1

transport

front 2

classify protein according to its function:
collagen, a major component of tendons and cartilage

back 2

structural

front 3

classify protein according to its function:
keratin, a protein found in hair

back 3

structural

front 4

classify protein according to its function:
amylases that hydrolyze starch

back 4

enzyme

front 5

classify protein according to its function:
insulin, a protein needed for glucose utilization

back 5

hormone

front 6

classify protein according to its function:
antibodies, proteins that disable foreign proteins

back 6

protection

front 7

classify protein according to its function:
casein, milk protein

back 7

storage

front 8

classify protein according to its function:
lipases that hydrolyze lipids

back 8

enzyme

front 9

what functional groups are found in all alpha amino acids

back 9

carboxylic acid an amino group

front 10

protein that consists of long, thin, fiber like shapes.

back 10

fibrous

front 11

proteins that make up structural tissues such as hair, wool, skin and nails

back 11

fibrous

front 12

proteins that have spherical shapes

back 12

globular

front 13

proteins that carry out the functions of the cells such as synthesis, transport and metabolism

back 13

globular

front 14

found in eggs, milk, meat, fish an poultry

back 14

essential amino acids

front 15

R is hydrocarbon or aromatic

back 15

nonpolar

front 16

hydrophobic

back 16

nonpolar

front 17

R contains polar molecule such as OH

back 17

polar

front 18

hydrophilic

back 18

polar

front 19

R contains COOH group

back 19

acidic

front 20

R contains NH2 group

back 20

basic

front 21

during ionization of amino acid the COOH group donates or accepts a proton?

back 21

donates

front 22

during ionization of amino acid the NH2 donates or accepts a proton

back 22

accepts

front 23

In solutions near neutral pH, most amino acids exist in the ionized form called the

back 23

Zwitterion

front 24

the Zwitterion has a net charge of

back 24

zero

front 25

in basic solutions the NH3 donates a proton thus forming an ion with a positive or negative charge?

back 25

negative

front 26

in acidic solutions the COO- accepts a proton thus forming a ion with a positive or negative charge

back 26

positive

front 27

in acidic solutions the COO- accepts or donates a proton

back 27

accepts

front 28

in acidic solutions the NH3 accepts or donates a proton

back 28

donates

front 29

peptide bonds can be broken by

back 29

hydrolysis

front 30

secondary structure is determined by

back 30

the amino acid sequence, the primary structure

front 31

folding of the primary structure into a specific shape

back 31

secondary structure

front 32

held together by H bonds between N-H and C=O

back 32

secondary structure

front 33

three main secondary structures shapes

back 33

alpha helix, beta pleated sheets and triple helix

front 34

coil with H bonds between N-H group and O of a C=O in the next turn

back 34

alpha helix

front 35

polypeptides held together side by side by H bonds to make sheets

back 35

beta pleated sheet

front 36

fibrous proteins such as silk

back 36

beta pleated sheet

front 37

hydrogen bonds form between oxygen atoms in the carbonyl groups of one polypeptide chain and the hydrogen atoms in the N-H groups of the amide bonds

back 37

beta pleated sheet

front 38

three polypeptide chains woven together like a braid

back 38

triple helix

front 39

held together by H bonds such as collagen

back 39

triple helix

front 40

most abundant protein in the body

back 40

collagen

front 41

located in fibrous proteins such as wool and hair

back 41

tertiary structure

front 42

helical chains coil together to form a structure like a rope and are held together by S-S bonds

back 42

tertiary structure

front 43

most proteins in the body are made what kind of proteins

back 43

globular

front 44

insulin, hemoglobin, enzymes and antibodies are all what kind of proteins

back 44

globular

front 45

proteins made of polypeptide chains that are folded into different secondary structures that are in turn folded into tertiary structure

back 45

globular

front 46

the tertiary structure of most globular proteins is the active or inactive form

back 46

active

front 47

the globular protein that stores oxygen in skeletal muscles

back 47

myoglobin

front 48

primary structure consists of polypeptide of 153 amino acids

back 48

myoglobin

front 49

tertiary structure is compact shape due to the folding of molecule to form a pocket for O2 to bind

back 49

myoglobin

front 50

the molecule is active only in its tertiary structure

back 50

myoglobin

front 51

tis formed when a globular protein is made of 2 or more peptide chains

back 51

quaternary structure

front 52

the peptide chains can be similar or different and are folded into its secondary and tertiary structure

back 52

quaternary structure

front 53

formed by the binding of the polypeptides in their tertiary structures together

back 53

quaternary structure

front 54

globular protein that transports oxygen to the blood

back 54

hemoglobin

front 55

protein that consists of 4 polypeptide chains or subunits

back 55

hemoglobin

front 56

how should the 4 subunits be held together in hemoglobin

back 56

by four different bonds like H bonds and S-S bonds in the quaternary structure

front 57

bond type of:
primary

back 57

peptide

front 58

bond type of:
secondary

back 58

H bonds

front 59

bond type of:
tertiary

back 59

H bonds and S-S bonds

front 60

bond type of:
quaternary

back 60

H bonds and S-S bonds

front 61

proteins in the primary and secondary structure are active or inactive?

back 61

inactive

front 62

proteins in the tertiary are active if

back 62

only one polypeptide is needed

front 63

proteins in the tertiary are inactive if

back 63

more than one polypeptide is needed

front 64

proteins in the quaternary structure are

back 64

active

front 65

the sequence of amino acids

back 65

primary

front 66

the coiled alpha helix, beta pleated sheet, or a triple helix formed by hydrogen bonding between peptide bonds along the chain

back 66

secondary

front 67

a folding of the protein into a compact, three dimensional shape stabilized by interactions between side R groups of amino acids

back 67

tertiary

front 68

a combination of two or more protein subunits to form a larger biologically active protein

back 68

quaternary

front 69

occurs when the bonds that stabilizes the secondary, tertiary or quaternary are disrupted

back 69

denaturation

front 70

a denatured protein is active or inactive?

back 70

inactive

front 71

denaturation agents

back 71

heat (above 50c)
acids and bases disrupt bonds
organic compounds
heavy metal ions
agitation

front 72

globular proteins that catalyze chemical reactions in the body

back 72

enzymes

front 73

active site is rigid

back 73

lock and key model

front 74

active site is flexible

back 74

induced fit model

front 75

factors affecting enzyme action

back 75

substrate concentration
temperature
pH