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