Bio Chapter 3

Front 1

How many pairs of electrons can carbon share?

Back 1

4

Front 2

What is the general role of enzymes?

Back 2

make reactions go faster, lower the activation energy of a reaction

Front 3

What are the 5 categories of reactions that are mediated by enzymes?

Back 3

rearrangement
cleavage
condensation
electron transfer
functional group transfer

Front 4

rearrangement

Back 4

a type of organic compound converted to another by changes in internal bonds

Front 5

cleavage

Back 5

molecule separted into two smaller compounds

Front 6

condensation

Back 6

covalent bonding between 2 small molecules - become bigger

Front 7

electron transfer

Back 7

electron splitting off from one molecules to another

Front 8

functional group transfer

Back 8

functionalgroup split off and transferred to another

Front 9

saturated vs unsatured

Back 9

saturated - all carbons have all their binding sites taken

Front 10

4 types of fats

Back 10

phospholipids
sterols
fatty acids
triglyceride

Front 11

amino acid

Back 11

a small organic compounds having an amino group, a carboxyl group, a hydrogen atom, and an R group

Front 12

peptide bond

Back 12

the kind of covalent bond linking one amino acid to another

Front 13

polypeptide chain

Back 13

three or more amino acids joined in a linear chain

Front 14

primary structure

Back 14

sequence of amino acids in a polypeptide chain

Front 15

proteins

Back 15

most diverse of all large biological molecules, some speed reactions, organism structure, nutritious, move substances, communication, defend against pathogens

Front 16

secondary structure

Back 16

twists, bends, loops, folds of polypeptide - formed by hydrogen bonds between R groups

Front 17

domain

Back 17

a polypeptide chain, or part of it, that has become a structurally stable unit -

Front 18

tertiary structure

Back 18

third level of protein organizations - makes the protein a functional molecules

Front 19

quaternary structure

Back 19

fourth level of protein organization - globular - multiple polypeptide chains

Front 20

heme group

Back 20

a large organic molecule with an iron atom at its center

Front 21

glycoproteins

Back 21

proteins with a sugar group attached

Front 22

lipoproteins

Back 22

proteins with a lipid group attached

Front 23

denaturation

Back 23

breaking weak bonds in larage molecules (such as protein) to disrupt three dimensional shapes such that they no longer function

Front 24

ATP

Back 24

adenonine triphosphate

Front 25

DNA

Back 25

deoxyribose nucleic acid

Front 26

RNA

Back 26

ribose nucleic acid

Front 27

coenzymes

Back 27

nucleotides necessary for enzyme function

Front 28

nucleic acids

Back 28

?

Front 29

base pairing

Back 29

?

Front 30

?

Back 30

?

Front 31

Functional groups - name and identify

Back 31

functional groups

Front 32

Where are hydroxl groups found? Do they dissolve in water?

Back 32

in alcohols (eg. sugars, amino acids) - water soluble

Front 33

Where are methyl groups found? Do they dissolve in water?

Back 33

in fatty acid chains - insoluble in water

Front 34

Where are carbonyl groups found? Do they dissolve in water?

Back 34

in sugars, amino acids, nucleotides - water soluble
At end of chain - aldehyde
In middle of change - ketone

Front 35

Where are carboxyl groups found? Do they dissolve in water?

Back 35

in amino acids, fatty acids -
water soluble - highly polar - acts as an acid (ie releases H+)

Front 36

Where are amino groups found? Do they dissolve in water?

Back 36

in amino acids and certain nucleotide bases -
water soluble
Acts as weak base (accepts H+)

Front 37

Where are phosphate groups found? Do they dissolve in water?

Back 37

in nucleotides (eg. ATP) also in DNA, RNA, many proteins, phospholipids -
water soluble, acidic

Front 38

What are functional groups?

Back 38

lone atoms or clusters of atoms that are covalently bonded to carbon atoms of organic compounds

Front 39

What is a saccharide?
Monosaccharide? Polysaccharide? Oligosaccharide?

Back 39

sugar
1 chain (monomer)
multiple chains (polymers)
short chain of sugar monomers

Front 40

What is sucrose?

Back 40

Disaccharide - fructose and glucose monomers

Front 41

What are the three most common polysaccharides (complex carbohydrates)

Back 41

cellulose, starch, glycogen

Front 42

cellulose

Back 42

glucose chains are stretched side to side - resist hydrolysis

Front 43

starch

Back 43

an angle to the next - coil like a staircase with hydroxyl groups to the outside - hydrolyzed easily for energy (plants)

Front 44

glycogen

Back 44

storage unit in animals - found in liver and muscles in particular

Front 45

chitin

Back 45

ni9trogen containing unit attached to glucose units - forms hard body parts and exoskeletons or many animals

Front 46

What are the different types of lipids

Back 46

fats
triglycerides

Front 47

What is a fat?

Back 47

one, two or three fatty acids attached to a glycerol molecule

Front 48

What is a fatty acid?

Back 48

backbone of as many as 36 carbon atoms, a carboxyl group at one end, and hydrogen atoms at most or all of the remaining carbons.

Front 49

What is the difference between saturated and unsaturated fatty acids?

Back 49

unsaturated - one or more double bonds (between two carbons)
saturated all single bonds

Front 50

What is the most abundant lipids in the body and what are they made up of?

Back 50

triglycerides - 3 fatty acid tails linked to a glycerol

Front 51

What are phospholipids?
What is their most important use?

Back 51

glycerol backbone, 2 nonpolar fatty acid tails, and a polar head.
Lipid bilayer for cell membrane.

Front 52

What are waxes?

Back 52

long-chain fatty acids tightly packed and linked to long-chain alcohols or carbon rings - plant cuticle, and eg. beeswax, birds secrete to make feathers waterproof

Front 53

What are sterols?

Back 53

no fatty acids
cholesterol, hormones

Front 54

What is an amino acid?

Back 54

small organic compound with an amino group (-NH3) a carboxyl group (COO-), a H atom and an R group - building blocks of proteins - 20 kinds

Front 55

What is a peptide bond?

Back 55

condensation reaction joins the amino group of one amino acid and the carboxyl group of the next in line

Front 56

What are the levels of protein organization?

Back 56

primary structure - sequence of amino acids
secondary structure - chain twists, bends, loops, and folds (hydrogen bonds)
tertiary structure - further bending, etc. gives protein it functional molecule ("domain")
quaternary - two or more polypeptide chains (eg. Hemoglobin)

Front 57

What are glycoproteins?

Back 57

saccharides attached to a polypeptide chain

Front 58

What is an example of a mutation in protein structure that results in a disease?

Back 58

Sicke cell disease.

Front 59

denaturation

Back 59

polypeptide chains lose their 3 dimensional shape and can no longer function - heat, changes in pH

Front 60

What are nucleotides?

Back 60

one sugar, at least on e phosphate group, and one nitrogen containing base - eg. DNA and RNA, and ATP

Front 61

What are the roles of nucleotides?

Back 61

energy transfer (transfer of phosphate group) eg ATP
coenzymes (necessary for certain enzympe reactions)
monomers for nucleic acids

Front 62

What are nucleic acids?

Back 62

Formed by a covalent bond getween the sugar of one nucleotide and the phosphate group of the next

Front 63

What are the 4 bases used in DNA?

Back 63

adenine, guanine, thymine, cytosine