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38 notecards = 10 pages (4 cards per page)

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Ch 2-5 test 1

front 1

What makes each element unique and different from other elements

back 1

Unique number of protons

front 2

What is the significance of atomic number

atomic mass?

back 2

Atomic number tells us the amount of protons in an atom

atomic mass tells us how many neutrons by subtracting the amount of protons

electrons can be found in the electron cloud. 1-2 On periodic table: electrons. 13-18 find by subtracting 10

front 3

What are isotopes

back 3

Variants of a particular element

different # of neutrons same # of protons

front 4

Atoms octet

back 4

If there are a certain number of electrons in an electron cloud you can either add or give away electrons to complete a perfect octet through sharing of electrons between elements

front 5

What are the max number of bonds specific elements can make?

back 5

Single H-H. Double bond= 2 pairs of electrons

double O= O. Triple bond= 3 pairs of electrons

triple N=_N

front 6

Define electro negativity

back 6

Level of charge given from one atom to attract another. Book Def: the attraction of a particular atom for the electrons of a covalent bond

front 7

How can electronegativity effect covalently bonded molecules

back 7

It takes partially greater charges from either positive and negatively bonded atoms and while shared equally, electrons will stay closer to the more electronegative charge

front 8

What happens if the electronegativity is equal

back 8

There is a standoff of tug of war and a non polar covalent bid is formed

front 9

What is the difference between ionic and covalent bonds?

back 9

Ionic bonds= electrons are not shared equally

covalent bonds= electrons are shared equally

front 10

back 10

Because it will gain one electron

front 11

Structure of water - hydrogen bond, polar covalent bond, explain in detail partial negative charge of water molecule and why it occurs in terms of electronegativity and electrons

back 11

Positive H in one H2O molecule attracts to negative O in another. Polar covalent bond = partially negative/positive binding in a covalent bond and the electrons stay closer to the more electronegative side

front 12

Importance of hydrogen bonding to the properties of water

back 12

Hydrogen bonds form the basic structure of water for other bondings such as polar covalent to occur

front 13

Why do carbon atoms form diverse molecules

back 13

Carbon has 4 valence electrons do it can share electrons with other diverse molecules

front 14

Hydrophobic molecules and how they interact with water

back 14

Hydrophobic doesn’t dissolve in water. It is no polar and does not have an attraction to water

front 15

Interpret a PH scale

back 15

1-6 Acid 7 neutral 8-14 basic

front 16

The importance of buffers in biological systems, how do they balance PH?

back 16

They maintain a relative constant PH when either acids or bases are added to them

front 17

The role of dehydration reaction in organic compounds and hydrolysis in digestion of organic compounds

back 17

Dehydratiom reaction: assembles polymers releasing H2O

Hydrolysis: breaks down polymers consuming H2O

front 18

The four macromolecules and bonds that are formed durning the dehydration reaction

back 18

Carbohydrates: glycoscidic linkage

Lipid: ester linkage

nucleic acid: phosphodiester linkage

protein: peptide bond

front 19

Classify monosaccharides, disaccharides, and polysaccharides

back 19

Monosaccharid: monomer of carbohydrate ex: lactose glucose

Disaccharide: two monosaccharides ex: sucrose

polysaccharid: polymers ex: plants -store glucose as starch, animals -glycogen, cell structure in plants -cellulose

front 20

The difference between starch and cellulose and how it impacts digestion

back 20

Starch: stores energy in plants. Plants and animals can digest

cellulose: structural component in plants. CANNOT be digested by animals on account of beta glucose linkage

front 21

What’s the difference between saturated and unsaturated fats

back 21

Unsaturated: liquid, at least on double bond

saturated: solidify, contains more hydrogen,only single bonds, contributes to atherosclerosis (heart disease)

front 22

What is the first structural level of protein? How can it change the activity of the protein

back 22

Primary: A mess up will ruin all other structures. It dictates secondary and tertiary structure. Linear chain of amino acids

front 23

Second structural level of protein

back 23

Secondary: hydrogen bonds between an amino group of one peptide bond and the carbonyl group of another peptide bond

front 24

Third structural level of proteins

back 24

Tertiary: interaction between r groups. Disulfide bridge, ionic bond, hydrogen bond between at least one r group

front 25

Fourth structural level of proteins

back 25

Quaternary: two or more polypeptide chains into one large protein

front 26

What makes each amino group different from one another?

back 26

Each has a different R group

front 27

Name the bonds that are formed in primary and secondary structures of proteins

back 27

Primary: peptide

secondary: hydrogen

front 28

Identify the peptide bond if given a polypeptide:

back 28

Carbon with a double bond to an oxygen single bonded to carbon attached to Nitrogen

front 29

What maintains structure of a protein

back 29

Hydrogen bonds

front 30

What is chaperonin

back 30

They help fold proteins within cells in the last structural level of proteins

front 31

Base pairing rules of DNA

back 31

A=T

C=G

front 32

Steroid structure

back 32

4 carbonn fused rings

front 33

back 33

front 34

Hydrocarbons are not soluble in water because

back 34

The C—H bond is nonpolar

front 35

What molecul a form a triacylglycerol/fat know and recognize the structure

back 35

G

l. Fatty acid 1

y

c

e. Fatty acid 2

r

o

L. Fatty acid 3

front 36

Bond between nucleotide to make nuclei acids - reaction forms it, type of bond

back 36

Phosphodiester covalent bond to form backbone from 5’ carbon and 3’ carbon

front 37

Recognize the the four biologically important organic compounds

back 37

Carbon

Hydrogen

Oxygen

Nitrogen

front 38

How do proteins reach their final shape

back 38

They go through all four phases and complete by using chaperonins