Chemistry- Proteins And Amino Acids

Front 1

what do enzymes regulate?

Back 1

biological reactions such as digestion and cellular metabolism

Front 2

what 2 functional groups do amino acids contain?

Back 2

amino group (NH2)
carboxylic acid group (COOH)
hydrogen bonded to central carbon

Front 3

alpha amino acids are what?

Back 3

COO-
NH3+
how they are in the body

Front 4

Classes of proteins

Back 4

structural
contractile
transport
storage
hormone
enzyme
protection

Front 5

Structural

Back 5

provide structural components
ex: collagen, keratin

Front 6

contractile

Back 6

move muscles
ex: myosin and actin

Front 7

transport

Back 7

carry essential substances throughout the body
ex: hemoglobin transports oxygen

Front 8

storage

Back 8

store nutrients
ex: casein stores protein in milk

Front 9

hormone

Back 9

regulate body metabolism and nervous system
ex: insulin regulates blood glucose level

Front 10

enzyme

Back 10

catalyze biochemical reactions in the cells
ex: sucrase catalyzes hydrolysis of sucrose

Front 11

Protection

Back 11

recognize and destroy foreign substances
ex:immunoglobulins stimulate immune responses

Front 12

non polar amino acids

Back 12

-hydrophobic

Front 13

polar amino acids

Back 13

-hydrophilic
-side chains such as OH, SH, and amide CONH2

Front 14

zwitterion

Back 14

-dipolar form of an amino acid
-net charge of zero

Front 15

solid amino acids have what boiling point?

Back 15

high because the zwitterion has the properties of a salt

Front 16

isoelectric point (pI)

Back 16

positive and negative charges are equal, which gives the amino acid an overall charge of zero
least soluble in solution, clumps together

Front 17

peptide bond

Back 17

amide bond that forms when COO- group of one amino acids reacts with the NH3+ group of the next amino acid

Front 18

dipeptide

Back 18

two amino acids linked together by a peptide bond form a dipeptide

Front 19

N-terminal

Back 19

amino group on left that is unreacted

Front 20

C-terminal

Back 20

carboxyl group on right that is unreacted

Front 21

protein

Back 21

when there are more than 50 amino acids in a chain, it is called a protein

Front 22

primary structure

Back 22

-the particular sequence of an amino acid in a peptide or protein
- determines the function of the protein
ex: Glu-His-Pro

Front 23

secondary structure

Back 23

-describes the way the amino acids next to or near each other along the polypeptide are arranged in space

Front 24

3 types of secondary structure

Back 24

alpha helix- corkscrew shape
beta pleated sheet-zigzags
triple helix- braid, most common is collagen, which is found in connective tissues, blood vessels, skin, etc

Front 25

tertiary structure

Back 25

-determines the 3D shape
-stabilized by interactions between R groups of amino acids

Front 26

stabilizing interactions of tertiary structures

Back 26

hydrophobic
hydrophilic (polar)
disulfide
salt bridge
hydrogen bonds

Front 27

hydrophobic

Back 27

interactions of two non polar groups

Front 28

hydrophilic

Back 28

interactions between two polar groups

Front 29

disulfide

Back 29

covalent bonds that form between the -SH groups of cysteines

Front 30

salt bridge

Back 30

ionic bonds between side groups of basic and acidic amino acids

Front 31

globular proteins

Back 31

have compact, spherical shapes because their secondary structures of the polypeptide chain fold over on top of each other
-functions such as synthesis, transport and metabolism

Front 32

fibrous proteins

Back 32

consist of long, thin, fiber-like shapes
-typically involved in the structure of cells and tissues

Front 33

quaternary structure

Back 33

when a biologically active protein consists of two or more polypeptide subunits
ex: hemoglobin

Front 34

denaturation

Back 34

occurs when there is a disruption of any of the bonds that stabilize the 2,3,4 structure
-primary is not affected
-globular protein unfolds

Front 35

5 ways of denaturation

Back 35

heat
acid and bases
organic compounds
heavy metal ions
agitation

Front 36

what do you need to hydroxylate?

Back 36

vitamin c

Front 37

3 structure is maintained by

Back 37

intrachain bonds:
hydrogen bonds, disulfid bond, hydrophobic interactions, salt bridges