Biology Unit 1

Front 1

non-polar covalent bonds

Back 1

when two atoms of equal size covalently bond or atoms are in balance with each other

Front 2

Why is water stable?

Back 2

weak bonds form between the partially charged oxygen of one atom and the partially charged hydrogen of another atom
-these weak bonds constantly form and rebreak in liquid medium
-though each individual bond is weak their combined effect is trong

Front 3

formation reactions

Back 3

anabolic reactions or anabolism
-polymers are formed when monomers are joined together by the removal of water, called dehydration synthesis

Front 4

breakdown reactions

Back 4

catabolic reactions or catabolism
-all molecules break apart when wate ris added, called hydrolysis

Front 5

monosaccharides

Back 5

glucose=universal cellular fuel, ATP gives us energy

Front 6

dissacharides

Back 6

sucrose in plants-used for transport of sugar (glucose and fructose)

Front 7

storage polysaccharides

Back 7

store fuel (glucose) by forming chains of it
-in animals=glycogen
in plants=amylose, amylopectin

Front 8

structural polysaccharides

Back 8

cross-branching makes water insoluble
cellulose= major component of plant cell walls
chitin=exoskeleton of arthropods

Front 9

formation of fats/lipids

Back 9

form via dehydration synthesis of 1 glycerol and 3 fatty acids to give 1 fat molecule (triglyceride)

Front 10

How energy is stored in fats

Back 10

energy is stored in C-H and C-C bonds, used when carbohydrates are low

Front 11

phospholipids

Back 11

dual polarity

Front 12

Primary structure of proteins

Back 12

linear sequence of AAs in any order, length, high diversity

Front 13

Secondary structure of proteins

Back 13

coils, pleats, caused by hydrogen bonding (h-bonds) that form between an amine group and the O of a carboxylic acid group

Front 14

alpha helix

Back 14

h-bonds within a single polypeptide chain. pulls the chain into a spiral or helical form

Front 15

beta pleated sheets

Back 15

H bonds form between many polypeptide chains

Front 16

tertiary structure

Back 16

driving force=hydrophobic interactions, R-group move away from water to interior

Front 17

bonds formed based on interactions of R-groups

Back 17

i. disulfide bridges- S-S
ii. H-bonds
iii.Vander Waals- weak, attractive charges
iv. ionic bonds- opposite charges

Front 18

domains

Back 18

areas on the folded protein that determine function. Includes more than one section of a single chain

Front 19

quaternary structure

Back 19

arises when more than one polypeptide chain binds to form a protein
-same interactions as with tertiary structures but between chains

Front 20

denaturation

Back 20

protein unfolding, loss of biological activity

Front 21

dissociation

Back 21

protein chains separate, when reunite protein is functional

Front 22

creationism

Back 22

special creation-God

Front 23

extraterrestril-panspermia

Back 23

cosmic dust

Front 24

spontaneous origin

Back 24

arising of organic molecules

Front 25

primitive atmosphere

Back 25

-Hot
-no free O2, yes=H2O, CH4, H2S

Front 26

carbohydrate monomer

Back 26

glucose=energy, saccharide

Front 27

Carb. dimer

Back 27

dissacharide
sucrose (table sugar)=transport in plants
lactose= (glucose and galactose)milk sugar

Front 28

carb. polymer

Back 28

strach=plants
glycogen= animal muscle tissue, energy storage
cellulose=structure in plants

Front 29

lipid monomer

Back 29

1 glycerol and 3 fatty acids

Front 30

lipid polymer

Back 30

triglyceride or fat, store energy, steroids=hormones

Front 31

Protein monomer

Back 31

amino acid

Front 32

protein dimer

Back 32

dipeptide

Front 33

protein polymer

Back 33

polypeptide, 6 functions

Front 34

nucleic acid monomer

Back 34

nucleotide

Front 35

nucleic acid polymer

Back 35

DNA, RNA
code, store information

Front 36

imbibition

Back 36

Absorption of fluid by a solid or colloid that causes swelling