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fall semester 2026
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why is chemistry necessary in biology
it provides the molecular foundations of life
determines comp, structure, function, interactions of bio molecules
defines chem rxn that provide energy, support, communation, and maintain life process
covalent bonds
atoms chemically combined in fixed numbers/ratios to form molecules of living and non-living matter
compounds
molecules whos component atoms are different (two or more atoms)
essential vs. trace elements
essential are those that an organism needs to live a healthy life and reproduce (20-25%) of natural elements
trace elements required in minute quantities
deficiency of essential elements
disrupts specific cellular processes, leading to characteristic physiological disorders
radioactive isotopes
undergo spontaneous nuclear decay, emitting particles and energy
used for medical diagnosis and fossil aging
radiation emitted can be detected and act as natural clocks
electrons and energy
electrons within an atom differ in the amount of stored (potential) energy they posess
the amount of energy determines where an electron is located around the nucleus
higher-energy electrons are generally farther from the nucleus
electron shells
energy levels
each has a characteristic amount of energy
orbitals
regions where electrons are most likely to be found within a shell
valence shell
outermost shell
atoms are most stable when the valence shell is full
if incomplete, the atom tends to gain/lose/share to become stable
covalent bonds
when atoms share a pair of valence electrons
strongest bond
nonpolar vs polar covalent bond
non polar the atoms share equally
polar one atom is more electronegative, not equal
electronegativity
the ability of an atom to attract electrons
ionic bonds
the electrical attraction between oppositely charged ions formed by electron transfer
ion formation
electron transfer creates oppositely charged ions ( cations and anions )
ionic bond formation
the + and - ions attract each other through electrostatic attraction
hydrogen bonds
when a hydrogen atom covalently bound to an electronegative atom (oxygen, nitrogen) interacts with an electronegative atom of another molecule
in living cells, the electronegative partners are usually oxygen or nitrogen atoms
where do hydrogen bonds form
between molecules with polar covalent bonds, where partially positive hydrogen is attracted to partially negative atoms in another molecule
van der waalls interactions
relatively weak electrical forces that attract molecules to one another
exist between virtually all atoms/molecules
stabilizes the shape of large molecules like proteins
molecule’s shape
determined by orientation of chemical bonds, which is determined by valence electrons
important for its function because of complementary molecular shapes with other bio molec
similar shapes = similar functions
water makes up ____ percent of a cell’s composition
70-95%
what does a water molecule contain
two hydrogen atoms covalently bonded to an oxygen
these covalent bonds are polar because oxygen is more electronegative than hydrogen
what are the poles of water molecule
because electrons are not shared equally:
partial negative pole near oxygen
partial positive pole near hydrogen
hydrogen bonds in water molecule
form between the slightly positive H of one water molecule and the slightly negative O of another water molecule
a water molecule can form up to ___ hydrogen bonds, and what are they?
four
two through its H atoms and two through the two lone pairs of electrons on its oxygen
four emergent properties of water
cohesive and adhesive (sticks to itself and others)
ability to moderate temperature
expansion upon freezing
versatility as a solvent
liquid water’s hydrogen bonds
constantly break and reform, allowing molecules to move closer together, increasing density
ice hydrogen bonds
form a stable, open crystal structure that keeps water molecules farther apart, reducing density
water vapor hydrogen bonds
mostly broken, allowing molecules to move independently and spread far apart, resulting in lowest density
water cohesion
hydrogen bonds holding water molecules together
creates strong interactions between water molecules, allowing water to maintain a continuous structure and resist derformation
adhesion
attraction between different substances
how does cohesion and adhesion help
the transport of water against gravity in plants
surface tension
resistance of the water surface to breaking, caused by cohesion between water molecules through hydrogen bonds
specific heat capacity
the amount of heat (joules) that must be absorbed or lost to change the temperature of a gram of a substance of 1 degree C
water has a high, so it cools and heats up more slowly than most substances
why does water have a high specific heat capacity
because of the large number of hydrogen bonds between water molecules
why is water a good temperature buffer
oceans can absorb or release a large amount of heat with only a slight change in its own temperature
density of ice vs water? why important?
the hydrogen bonds are stabilized so that the average distance between water molecules is less than in liquid water
this means ice is less dense than water and therefore floats on top of it
if it sunk, all bodies of water would eventually freeze solid, life would be impossible
water reaches its greatest density at
4 degrees C
water is the _____ of life , why?
solvent
due to its polarity, large variety of molecules can be dissolved
hydrophillic molecules
can be dissolved in water
form hydrogen bonds or ion-dipole interactions with water that allow them to
hydration shell
a sphere of water molecules that surrounds each ion of an ionic compound when dissolved in water
pH
a logarithmic measure of the concentration of hydrogen ions in a solution
negative logarithimic scale, meaning a higher pH means a lower H+ concentration
acidic/neutral/basic pH
acidic: less than 7 pH, high concentration of H+
neutral: 7, equal H+ and OH-
basic: higher than 7, low H+
pH of pure water
a hydrogen atom in a hydrogen bond between water molecules can shift from one molecule to the other
the hydrogen atom leaves its electron behind, and is transfered as a proton, or a hydrogen ion
the molecule with the extra proton is now a hydronium ion (H+)
the molecule who lost the proton is now a hydroxide ion
dynamic equillibrium
which water molecules disassociate at the same rate in which they are being formed
buffers
substances that minimize changes in the concentration of H or OH in a solution or in a living cell
acid-base pair
in buffers that can exchange protons
why does carbon dominate life (6)
small enough to form strong covalent bonds
large enough to bond with many different atoms
tetravalent, allowing four simultaneous covalent bonds
stable enough to preserve complex structures
reactive enough for metabolism
compatible with liquid water
structure-function relationship
different molecular shapes
different chemical properties
diffferent biological functions
greater biological comeplexity
hydrocarbons
molecules composed of only carbon and hydrogen
four ways the carbon skeleton can vary in hydrocarbons
length ( number of carbon atoms in the chain)
double bond position
branching (side chains attached to main carbon chain)
presence of rings (carbon atoms joined in a ring structure)
isomers
molecules with the same molecular formula but different molecular structures
different chem and bio properties s
structural isomers
have the same molecular formula but different structural formulas because their atoms a
cis-trans isomers
same molecular formula, same structural formula (connectivity of atoms), different spatial arrangement (configuration) of atoms
differ in the three dimensional arrangement of functional groups due to restricted rotation around a double bond
functional groups are arranged on the same side (cis) or on the opposite side (trans)
enantiomers
differ in the three-dimensional arrangement of functional groups caused by chirality (an asymmetric carbon)
produces mirror image molecules
same formula and connectiveity
all amino acids except glycine….
have a L and D enantiomer
only the L form is used in biological system
differences between two enantiomers
if a drug may have different effects
structure-function relationship
functional groups
determine chemical properties and bio activity
specific arrangement of atoms that confer unique properties to molecules and are often involved in chemical rxn
seven functional groups most important for life
hydroxyl
carbonyl
carboxyl
amino
sulfhydryl
phosphate
methyl
4 classes of biological macromolecules
protein, libids, carbs, nuleic acids
polymer
long molecule consisting of many similar building blocks
monomer
small building block molecules that make up polymers
dehydration reactions
how polymers are synthesized
water is a product of the rxn
hydrolysis reaction
how polymers are dissassembled
the reverse of dehydration rxn
monosaccharides
simplest carbs
disaccharide
linking only two monosaccharides together
polysaccharide
function: fuel and structural materal
structure: long chains of monosaccharides linked together
both determined by monosaccharide composition and glycosidic linkage positions
naming, structure, and formula of monosaccharides
multiples of CH2O (ratio of 1:2:1)
simple sugars end in -ose, named based of the number of carbons
can exist in a linear or ring form, all have a C=O bond when in linear form
classification of monosaccharides
aldoses - contain aldehyde group
ketoses- contains a ketone group
gluce vs galactose vs fructose
glucose is the primary cellular fuel
galactose and fructose are converted to glucose before most cells use them
glycosidic linkage
the covalent bond linking disaccharide
glucose, galactose, and fructose can be combined to form…
maltose, lactose, and sucrose
for specific biological functions, such as transport storage or nutrition
alpha vs beta glycosidic bond
differ in the orientation of the glycosidic bond at the anormeric carbon
anormeric carbon
carbon of the carbonyl group (aldehyde or ketone) in the linear form
starch
a polymer of glucose
used by plants to store glucose
the simplest form: amylose
glycogen
a polymer of glucose, and is used by animals to store glucose
cellulose
polymer of glucose, used by plants to make strong cell walls
how can cellulose, starch, and glycogen have such different properties?
glycosidic linkages
microfibrils
straight cellulose polymers that can H-bond with each other
parellel cellulose molecules which form strong building materials for plants
lipids
not polymers, but are all hydrophobic
3 major types of lipids
triacylycerols (ex fats and oils)
phospholipids (ex cell membranes)
steriods (ex sex hormones)
triacylglycerols
neutral fats
energy storage, insulation, and protection of internal organs
three fatty acid chains attached to a glycerol
glycerol
a three carbon alcohol (three hydroxyl groups)
fatty acids
a hydrocarbon with a carboxyl group at the end
vary in length and the number and location of double C=C bonds
ester linkage
how a fatty acid connects to a glycerol
saturated fatty acids
no C=C double bonds
unsaturared fatty acids and 2 types
one or more C=C double bonds
monounsaturated: 1 double bond
polyunsatured: 2 or more double bonds
triacylglyerols
containing mostly satured fatty acids
usually solid at room temperature (eg butter)
straight hydrocarbon chains pack tightly together
omega-3 fatty acids
unsaturated fatty acids that are not synthesized in human body
must be supplied in diet
how can we compare energy in macromolecules
by meauring how much energy is stored in 1g of each
phospholipid molecules
major constituent of cell membranes and cell signaling
2 fatty acid chains
1 glycerol molecule
1 phosphate molecule
amphipathic phospholipids
having both hydrophobic and hydrophillic parts of the molecule
when placed in water, phospholipids….
self-assemble into a phospholipid bilayer
shield their hydrophobic tails from water
steroids
constituents of cell membranes (e,g) cholesterol
components of vitamins and hormones
structure: made from sterol, four carbon rings composed of 20 covalently bonded C atoms
proteins
highly diverse, workhorses of most cellular functions
polypeptides made of amino acids subunits
enzymes
act as catalysts, increasing the rate of chemical rxns
structural proteins
provide structural support and shape to tissues, such as collagen
motility proteins
drive muscle contraction and cell movement
regulatory proteins
control and coordinate cell functions
transport proteins
move substances in and out cells