bio

describe water diagram

describe water diagram

oxygen is negative and hydrogen end is positive

*know how to draw

charged regions can attract each other creating hydrogen bonds

oxygen and hydrogen are bonded through covalent bonds

cohesion

attraction of water to itself

cohesive forces are attempting to pull the water into the smallest possible sphere

surface tension is caused by this as the water is attempting to stick together through cohesive forces while an object is penetrating the surface

adhesion

due to polarity caused by hydrogen bonds

attraction of water to other substances

water is

water tends to stick to other charged substances

large number of hydrogen bonds gives forces strength

explains how water “defy” gravity as it is bonding to surface

capillary action

caused by combination of adhesive and cohesive forces where water can travel along a charged medium against gravity to a degree. water binds the sides and water binds to itself causing it to slowly go along the material

solvent

water can act as a good solvent because the large amount of polar attraction between water molecules interrupt intermolecular forces such as ionic bonds and cause the atoms to break down

things that are hydrophillic

polar molecules, charged molecules, substances that water adheres to

things that are hydrophobic

nonpolar molecules, noncharged molecules, substances that dissolve in other solvents, lipids

molecules that can freely travel through the blood stream

glucose (polar molecules), amino acids (acid groups are charged, but R group may or may not be so this determines degree of solubility), sodium chloride (ionic)

molecules that need something else

fats (nonpolar so carried through lipoprotein complex), cholesterol (hydrophoic so carried through lipoprotein complex)

oxygen (non-polar but soluble as temperature decreases; body temperature too high so hemoglobin in red blood cells carry the oxygen)

lipoprotein complex

outside layer is phospholipid molecules with hydrophillic phosphate heads facing outwards

thermal properties of water

high specific heat capacity

high heat of vaporization

high heat of fusion (amount of energy lost to change liquid water to ice)

reason: many hydrogen bonds need to be broken or formed to change temperature of water

water as coolant in sweat

high temperatures causes enzymes to denature

when water is on skin, takes lots of energy to heat water up so skin underneath is safe

when water is evaporated, lots of energy is removed

skin and blood vessels are cooled

water makes up most of the body, so the body is relatively resistant to heat change. If one part of the body is cool, the cool blood will travel to other parts to cool it down

main difference between methane and water

methane is non-polar and water is polar

why can we not say that water has memory

some dumbasses put antibodies in water and saw a reaction did serial dilution and saw the same thing

many people tried to repeat it but it didn’t work and too small population

pseudoscience - they didn’t follow scientific method

4 most common elements in living organisms

carbon, hydrogen, nitrogen, and oxygen

role of other elements

nitrogen - protein

sulfur - protein

potassium - transmit nerve impulses

sodium - transmit nerve impulses

iron - found in hemoglobin

calcium - teeth and bones

phosphorus - found in nucleic acid, ATP, and cell membrane structures

why is carbon able to form macromolecules

has 4 valence electrons so can form 4 covalent bonds

metabolism

- all enzymatic reactions in body

anabolism

- synthesis of macromolecules from simpler molecules (H2O removed to form bonds) ex: lactose

catabolism

• macromolecules being broken down to release energy, ex: digestion, cell respiration

KNOW TO DRAW WATER MOLECULE

why is water polar

unequal sharing of electrons and unsymmetrical shape of molecule

carbohydrates

monosaccharide

lipids and fats

fatty acid

nucleic acid

nucleotides

protein

aminoi acids

why is carbon so important

has four valence electrons so it can form 4 covalent bonds

vitalism

theory that living organisms are alive because of a vital principle distinct from chemical forces

how was vitalism falsified

urea: excretes excess amino acids

organic compounds could be created in lab

carbohydrates

carbon compounds consisting of one or more simple sugars (CH2O)

glucose

monosaccharide that is the basic unit of many polymers

respiration to produce ATP

galactose

also a hexose sugar but less sweet

ribose vs deoxyribose

pentose sugar and backbone of RNA

bottom right if OH is ribose if H is deoxyribose

fructose

sweetest naturally occurring carbohydrate

energy source of fruits and honey

triglyceride formation

3 fatty acid and glycerol

lipids hydrolysis

glycerol and fatty acids

lactose conformation

galactose and glucose

energy source in milk

sucrose formation

glucose and fructose

convenient form of transferring water throughout the plant

maltose

disaccharide of 2 glucose molecules

glycogen

repeating glucose subunits branched

short term energy storage in liver and muscles

starch

major carbohydrate reserve

contains several million amylopectin molecules with many smaller amylose molecules

cellulose

repeating glucose units linear

multiple hydrogen bonds form between strands creating microfibrils

structural component of cell wall

lipids

fats, oils and waxes

biological fuels, hormones, and structural components of membranes

not macromolecules

nonsoluble in water but soluble in nonpolar solvents

neutral fats

most common lipid with ester links

saturated fatty acid

maximum number of fatty acids

no double bonds

straight chains

solid at room temperature

unsaturated fatty acid

some carbon atoms are double bonded

liquid at room temperature

kinks in straight chains

cis isomers

commmon in nature

hydrogen atoms are on same side of the two carbon atoms

double bond causes bend

loosely packed

low melting points

trans isomers

rare in nature (margarine from vegetable oils)

opposite side of the 2 carbon atoms

double bond does not cause bend in fatt acid chain

tightly packed

high melting points

common lipids

oleic acid, a-linolenic acid, and caproic acid

phospholipid

one fatty acid group of triglycerol is replaced with a phosphate group

glycerol molecule, two fatty acid chains, and a phosphate

steroids

three 6 carbon atom rings and one 5 carbon atom ring

examples: sex hormones, hormones such as cortisol and aldosterone, and cholesterol

triacylglycerols (triglyceride)

glycerol is an alcohol containing 3 carbon bonded to a hydroxyl group

hydrolysis will break down triglycerides into subunits

lipids functions

structure: phospholipids are main component of cell membrane

hormonal signaling: steroids

insulation: fats serve as heat insulators

protection: triglycerides form tissue layer around many key internal organs and provide protection against physical injury

storage of energy

triglycerides are used as long term energy source

energy ratio

fat:carb:protein

2:1:1

bmi

identify possible weight problems

=mass (kg) / height (m^2)

kg/m^2

monogram: draw line from weight to height using ruler to see where it intersects

proteins

made up by amino acids

shaped based on sequence of amino acids

acid amino acids charge

basic amino acids charge

negative

positive

start codon

AUG (methiomine)

R groups

give amino acids their properties

acidic vs basic

polar vs nonpolar

hydrophillic vs hydrophobic

what is responsible for sequence of amino acids

genes

polypeptide formation

2 amino acids bonded together

peptide bond is formed between carbon and nitrogen

what determines function of protein

structure

primary structure

amino acid sequence linked by peptide bonds

interaction between R groups of amino acid determines shape

what is shape of protein

conformation

secondary structure

shape of polypeptide chain

shape is result of hydrogen bonds

2 common shapes of secondary structure

alpha helix coils

beta-pleated sheets

tertiary structure`

the protein’s fold

folds with the help of chaperone proteins and interactions between R group

hydrogen bonds, hydrophobic interactions, ionic interactions, disulfide bridges

determines function

quaternary structure

not all proteins have this

those that do have polypeptides that aggregate together

ex: hemoglobin

why can proteins perform a variety of functions

quartenary and tertiary structures

fibrous protein

long and narrow

structural

genearllly insoluble in water

less sensitive to changes in heat, pH etc.

collagen

globular protein

rounded and spherical

functional

generally soluble in water

more sensible to heat, pH

catalase

rubisco

fixes carbon dioxide from the atmosphere

enzyme

insulin

hormone - signals cells to take and absorb glucose

immunoglobulins

antibodies

respond to huge range of pathogens

provokes an immune response

rhodospin

pigment that absorbs light

collagen

rope-like proteins

quarter of all protein in the human body

give strength and structure to various parts of the body

spider silk

extensible and resistant to breaking

genome

genes of organism that gives an idea of what the proteome could be

environment factors

influences proteins needed based on surroundings

proteome

proteins produced by organism that reveals what is happening at a certain point in time

denaturation

when proteins are outside a specific range of temperature and pH

interruption of bonds which means interruption of structure which means interruption of function

temperature

as heat energy increases, molecules within the bonds vibrate violently breaking bonds

pH

pH measures amount of free-flowing H+ ions there are

when one of the H+ ions attaches to the amino acid, charge is changed thus breaking bonds and denaturing

enzyme

globular proteins that speed up reations by lowering the activation energy threshold

induced fit model vs lock and key model

enzyme changes shape slightly to put stress on bonds vs fits perfectly

collision theory

in order for enzymatic action to coccur, enzymes must come into contact with substrate

when heated, easier to combine because enzymes move faster meaning more chance to collide

common uses of enzymes

lactose, restriction enzymes, pcr reactions, and detergent

immobilized enzymes

attached to material so their movement is restricted

advantages

Concentration of substrate can be increased as enzyme will not dissolve

Recycled enzymes can be reused, enzymes can be separated easier

O

Separation of products is straightforward and easier

Stability is increased with more resistance to temperature and pH changes

lactose milk produced

lactase beads, milk is poured through repeatedly, lactase breaks lactose into glucose and galactose

result: sweetened

reduce crystalisation of ice cream

shorten production time for yogurt and cheese

how do enzymes lower activation energy of reaction

due to binding, bonds in substrate are stressed

progresses reaction

lowers overall energy level of transition state

activation state is reduced

normal enzyme graph

example of competitive inhibition

relenza

example of noncompetitive inhibition

cyanide

anabolic

small molecules are used to create larger ones

condensation

synthesis

endothermic

two substrates enter an enzyme which creates chemical bonds to connect them

need energy

catabolic

break down larger molecules into smaller subunits

exothermic

one substrate into 2

metabolic pathways (essay)

body requires several reactions to produce required product

metabolic pathways consist of chains and cycles of enzyme-catalyzed reactions

end product inhibition

there is enough end product and the metabolic pathways shut down

end product will bind to first enzyme allosterically to inhibit the enzyme until it is needed again

threonine into isoleucine

when there is too much isoleucine end product, isoleucine travels back to the first enzyme and inhibits it until there is low concentrations of isoleucine again