Chapter 4

inorganic compounds

do not usually contain carbon
-H2O, CO2, salts, bases, and HCl

organic compounds

-contain carbon
-almost always contain oxygen and nitrogen
-usually contain oxygen and nitrogen
-may also contain phosphorous, sulfur, and small amounts of calcium, iron, sodium, chlorine, potassium

60-80% water

how abundant is the inorganic compound water in our body

high heat capacity, high heat of vaporization, polar molecule, important reactant, cushioning

properties of water

high heat capacity

absorbs and releases large amounts of heat before its temperature changes appreciably

high heat of vaporization

to evaporate, water requires large amounts of heat energy to disrupt the hydrogen bonds that hold water molecules together

polar molecule

water molecules are formed by polar covalent bonding, which results in water molecules exhibiting a positive end/pole, and a negative end/pole
-also gives water the ability to dissolve many substances (universal solvent)

important reactant

water in many chemical reactions
-hydrolysis
-dehydration synthesis

cushioning

water forms a cushion (due to hydrogen bonding) around certain body organs to protect them from physical trauma
-ex: amniotic fluid which surrounds fetus in mother's body and plays a role in protecting mother

latent heat affect

releases energy slowly for all energy taken in

adhesion

water will stick to other things

cohesion

water will stick to another water molecule

salts

-ionic compounds consisting of cations other than H+ and anions other than OH-
-most abundant are ____ containing Ca++ and PO4^3-
-others include Na+, K+ (important for nerve impulses) and Fe^3+ which forms part of hemoglobin molecule that transports oxygen within red blood cells

heme

makes Fe^3+ a hemoglobin when put with red blood cells

affinity

Fe is attracted to carbon monoxide, oxygen, carbon dioxide

electrolytes

substances that conduct electrical current while in solution
-all salts are these

parabolic chamber

increases atmospheric pressure then releases it slowly

acids and bases

ionic compounds that dissociate in water to yield either H+ or OH-

acids

yield H+ in water
-have a sour taste
-proton donors

bases

yield OH- in water
-have a bitter taste
-proton acceptors

neutralization

when acids and bases are mixed they chemically react to form a salt and water
-exchange reaction
-if hydrogen donates an electron, it becomes H+ (cation because of positive charge), then is naked proton because that was its only electron

pH

the relative concentration of hydrogen/hydroxide ions in a solution

pH scale

used to express the concentration of hydrogen ions
-runs from 0-14
-low pH corresponds to high hydrogen ion concentration (importance of pH in blood and delivery of oxygen to tissue)
-high pH is when alkaline neutralizes acidic body

7.35-7.45

normal blood pH range

electroneutral (always shares electrons), four valence shell electrons, can form chainlike molecules and ring structures

3 reasons why carbon is important

biosynthetic organic compounds

organic compounds made in the bodies of living things
-carbohydrates
-lipids
-proteins
-nucleic acids

carbon, hydrogen, oxygen

make-up of carbohydrates

C:H:O 1:2:1

ratio of carbohydrates

Cn(H2O)n

formula of carbohydrates

monosaccharide

one sugar carbohydrate

oligosaccharides

few number of sugars carbohydrate chain

polysaccharides

many sugars carbohydrate

monosaccharides

-simple sugars
-3-7 carbons

glucose

-main sugar metabolized by the body and used for energy
-common monosaccharide
-aka: dextrose, bland

fructose

-converted to glucose by the liver when consumed
-common monosaccharide
-aka: fruit sugar, sweet/sugary

galactose

-not normally found in nature, but combines with glucose to form lactose (milk sugar)
-common monosaccharide
-bland

oligosaccharides

-short chain carbohydrates that consist of from 2-10 monosaccharides (30-70 carbons) linked together by covalent bonds
-broken down by digestion into simple sugars

disaccharide

when two monosaccharides combine

sucrose

glucose and fructose; disaccharide

lactose

glucose and galactose; disaccharide

maltose

glucose and glucose; disaccharide

polysaccharides

-most complex type of carbohydrate
-aka: glycans
-long chain of glucose units (300-1000)

starch

highly branched polysaccharides

glycogen

-animal starch
-stored in skeletal muscles and liver

cellulose

unbranched (long chain) polysaccharide
-insoluble in water
-can not be digested
-can be called roughage/fiber
-stimulate peristalsis- wavelike contractions that move food through the digestive system

carbon, hydrogen, oxygen

make up of lipids
-sometimes nitrogen, sulfur, and phosphorous too

H:O is greater than 2:1

ratio of lipids

fats (neutral lipids), phospholipids, steroids, waxes

types of lipids

fatty acids

-building blocks of lipids
-carbon chains of varying lengths with an acid group attached at one end

saturated, unsaturated, and polyunsaturated

types of fatty acids

saturated fatty acid

all available carbon bonds are filled with hydrogen atoms

unsaturated fatty acid

-not all available carbon bonds are filled with hydrogen atoms
-one or more double bonds exist in the carbon chain

saturated fatty acid

solid at room temperature because they are packed together

unsaturated fatty acid

fatty acid where double bond allows the fatty acid chain to break easier, is better for you

polyunsaturated fatty acid

more than one double bond in the fatty acid chain

ester linkage

joins acid and alcohol (carboxyl group of fatty acid and glycerol) together and creates a water molecule

cis fatty acid

-hydrogens are all on the same side of the double bond of unsaturated fatty acid
-more easier to break

trans fatty acid

-hydrogens are both up and down on unsaturated fatty acid chain

cis fatty acids

-protects us from inflammation/swelling
-lowers cholesterol levels
-omega 3's (double bond after 3rd carbon in chain)
-have kink so that enzyme can break down easier
-important for nice hair, reproductive issues, healthy bones, and protection from heart disease

trans fatty acids

-hydrogenated artificially
-bad for you
-associated with low density lipoprotein cholesterol and coronary heart disease
-rarely occur naturally
-enzymes have trouble binding with them and breaking them down
-remain solid in the body
-go into blood stream and clog coronary arteries

neutral lipids (fats)

-comprised of glycerol molecule and 3 fatty-acids
-most abundant lipids in the body
-important sources of energy reserve when oxidized through respiration
-protects deeper organs
-stored in adipose cells

neutral lipids (fats)

medical community calls them triglycerides

saturated fats

-neutral lipid
-aka: animal fats
-solid at room temperature
-hard to digest and raises blood cholesterol levels
-not essential to health
-found in some plant foods (coconut, coconut oil, palm oil)
-packed tight- no kinks

unsaturated fats

-neutral lipid
-aka: oils
-liquid at room temperature
-monounsaturated, polyunsaturated fatty acids
-have kinks (double bonds)

carbon, hydrogen, oxygen, phosphorous

makeup of phospholipids (elements)

glycerol, 2 fatty acids, phosphate group

makeup of phospholipids (parts)

phosphate group

head of a phospholipid and is polar (hydrophilic)

fatty-acid chains

make up the phospholipid tail and are nonpolar (hydrophobic)
-nonpolar attracts other nonpolar

micelle

what do phospholipids form when in water

lipid bi-layer (phospholipid bilayer)

principle components of cell membranes

steroids

flat molecules formed from four interlocking rings (steroid nucleus) attached to a fatty-acid chain

1 cyclopentane ring and 3 cyclohexane rings

what makes up the steroid nucleus

cholesterol

most important steroid

cholesterol

-in all cell membranes
-enters body through diet
-produced by the liver
-keeps the phospholipid bilayer fluid
-needed for digestion
-used to make vitamin D and some hormones (sex hormones, cortisol, estrogen, etc.)

proteins

most abundant biosynthetic organic compounds in cells

carbon, hydrogen, oxygen, nitrogen

makeup of proteins
-sometimes sulfur, phosphorous, iron
-50% of organic matter in the body

amino acids

building blocks of proteins

amino acids

-distinguished by its R group
-20 different
-bonded together in proteins by peptide bonds

peptide bonds

-bond amino acids together in proteins
-specialized covalent bonds

hair and nails, blood, brain and nerves, enzymes, cellular construction workers, antibodies, cellular messengers, muscles

what proteins can help/affect

alpha carbon

-central carbon where everything else is based
-at least one hydrogen attached
-beginning carbon

aromatic

ringed structure of amino acid

22

technical number of different amino acids, but only 20 are used in constructing proteins

protein structure

can range from as little as 50- thousands of amino acids in length

peptide bonds

formed by dehydration synthesis between carboxyl group of one amino acid (the OH) and the amine group of another (the H)

primary structure

-a protein's amino acid order
-proteins don't usually exist in this form
-not functional

secondary structure

two types that make up this protein structure are alpha helix and beta-pleated sheet

alpha helix

-spiral- shaped protein structure
-formed by primary structure coiling

beta-pleated sheet

-fan-folded shaped protein structure
-linked side by side with hydrogen bonds
-primary polypeptide chains do not coil

tertiary structure

-full 3-D folded protein structure
-biologically active form
-proteins must achieve at least this form to function

fibrous and globular

types of tertiary structure

fibrous

-aka: structural protein
-have extended rope-like structure
-NOT water soluble
-ex: collagen (found in bones, cartilage, tendons, keratin)

globular

-aka: functional protein
-compact, somewhat spherical shape
-water soluble
-generally non-structural enzymes

quaternary structure

-two or more tertiary structures bonded together
-looks like congealed clump of pasta
-biologically active form
-some proteins (hemoglobin- globular and collagen- fibrous)

water-loving

what amino acids will stay near the surface of protein

water-fearing

what amino acids will be buried in the protein's core

denature

when a protein loses its 3-D shape

denature

-protein is no longer able to perform physiological roles
-hydrogen bonds are weak and easy to break
-can be caused by environmental changes, such as high temperature
-loss of 3-D shape means loss of function

fibrous

stable structural proteins

globular

not stable proteins