BIO MASTER (3)

sticky wicky

cohesion, adhesion

cohesion/adhesion importance

surface tension, capillary action

capillary action

transport fluid through plants and body

not so hot

high specific heat

specific heat capacity importance

maintain homeostasis, climate temp is regulated

floats when frozen

ice floats

ice floating importance

bodies of water don’t freeze solid

dissolves a lot

universal polar solvent

solvent importance

solutes can dissolve and be transported easily

cohesion

water sticks to water thru polarity and h bonds

surface tension

how difficult it is to break the surface of a liquid

adhesion

water sticks to other charged molecules

capillary action

water moving up small tubes via adhesion

transpiration

evaporative water loss from a plant

hydrophobic

non-charged, nonpolar, substance repels water

hydrophillic

charged, polar, attracts water via adhesion

high specific heat

takes lot of energy to heat water, have to break h bonds

water has high boiling point

can absorb/release large amt of energy w/ little temp change

solid water less dense than liquid

h bonds cause frozen molecules to space out

water freezes at top

life exists under ice layer

solution

liquid homogenous mixture of substances

solvent

dissolving agent, liquid

solute

substance being dissolved, solid

hydration shell

sphere of water molecules around polar ions due to polarity

monomer

small building blocks

polymers

2+ monomers linked

carb monomer

monosaccharide, glucose

carb polymer

carbohydrate, disaccharide

fat polymer

lipids

protein monomer

amino acid, peptide

protein polymer

protein, polypeptide

nucleic acid monomer

nucleotide

nucleic acid polymer

DNA, RNA

dehydration synthesis

join monomers, water is released

hydrolysis

break monomers apart, water is added

carbs function

energy, storage, structure, genes

carbs energy

cellular respiration

carb storage

glycogen, starch

carb structure

chitin, cellulose

carb genes

deoxyribose, ribose

monosaccharides

1 carbon ring (fructose, glucose, galactose)

carbon ring

C₆H₁₂O₆

disaccharides

2 carbon rings (lactose, sucrose, maltose)

oligosaccharides

3-9 carbon rings, found on cell membranes

polysaccharides

10+ carbon rings (glycogen, cellulose, amylose)

lipid properties

nonpolar, hydrophobic

lipid types

triglycerides, steroids, waxes, phospholipids

triglycerides structure

3 fatty acids bonded to glycerol

triglyceride function

long term energy, insulation, cushioning

saturated fat

no double bond, saturated w/ H, straight chain, solid at room temp, animal based

unsaturated fats

carbon double bond, kinks in chain, liquid at room temp, plant based

trans fats

hydrogenated unsat fats, solid at room temp, unhealthy

phospholipid stucture

phosphate, glycerol, 1 sat fat tail, 1 unsat fat tail

phospholipid function

phospholipid bilayer semipermeable membrane, hydrophillic heads/hydrophobic tails

steroid structure

4-5 carbon rings, hydrophobic

steroid function

metabolism, immune response, sex hormones

wax structure

fatty acid w/ alcohol

wax function

prevent water loss

protein function

enzyme, structure, carriers, communication, defense, movement

enzyme

speed up chemical reaction (DNA polymerase)

structure

keratin, collagen

carriers/transporters

hemoglobin

cell communication

receptors, signals (insulin, hormones)

defense

antibodies

movement

actin, myosin

amino acid structure

central carbon, r side chain, carboxyl, amine, H

amino acid table

20 amino acids (64 possible combos)

polypeptides

aa bonds thru dehydration synthesis

peptide bond

covalent bond found in proteins

side chain types

nonpolar, polar, charged

nonpolar side chain

hydrophobic, lots of CH

polar side chain

hydrophilic, OH & N, bond with each other or water

charged side chain

hydrophilic, acidic: negatively charged H+ donors, basic: positively charged H+ acceptors

primary structure

order of amino acids in chain, single change has big effects

primary structure stabilizer

peptide bonds

secondary structure

local folding into alpha helices and beta pleated sheets

secondary structure stabilizer

H bonds with carboxyl and amine

tertiary structure

interactions btw distant AAs, 3D shapes, nonpolar cluster inwards

tertiary structure stabilizers

h binds, ionic bonds, disulphide bridges

quaternary structure

more than 1 polypeptide chain bonded together

protein denaturation

unfolding due to disruptions in H and ionic bonds (pH, temp, salinity), destroys functionality

nucleic acid function

code for amino acid sequence in proteins

nucleotide structure

pentose sugar, phosphate, nitrogenous base

DNA structure

deoxyribose sugar, double helix, ATCG

RNA structure

ribose sugar, single strand, AUCG

pyramidine

single ring

purine

double rings

Adenine

purine, 2 bonds

thymine

pyramidine, 2 bonds

guanine

purine, 3 bonds

cytosine

pyrimidine, 3 bonds

antiparallel

strands run in opposite directions due to h bond structure

5’ 

top carbon in deoxyribose joined to P group

3’

bottom of sugar

evolution

change in genetic composition of a population from generation to generation

darwin’s observations

• populations have varying traits

• traits are heritable

• not all offspring survive into adulthood due to limited resources

darwin’s conclusion

individuals with traits advantageous in survival and reproduction are able to have more offspring, leading to the accumulation of advantageous traits in future generations

adaptation

inherited characteristic that enhances survival/reproduction in specific environments

coevolution

reciprocal evolution between interacting species

macroevolution

big evolutionary changes over long periods of time; above species