Atom
smallest unit of matter
contains a nucleus and an electron cloud
composed of subatomic particles
join together to form molecules
Ionic Bonds
attractions between cations (electron donor) and anions (electron acceptor)
Cation
positively charged ion
anion
negatively charged ion
covalent bonds
involves sharing electrons
Hydrogen bonds
weak polar bonds based on partial electrical attractions
Decomposition reactions
breaks down chemical bonds
AB→ A + B
Hydrolysis
“water loosening or breaking”
ABCDE + H2O→ABC -- H + HO -- DE
Catabolism
breakdown of complex molecules withing body cells that produces energy
--CD → C + D + energy
Synthesis Reaction
Forms chemical bonds
A + B → AB
Dehydration Synthesis (condensation)
formations of a water molecule
ABC-- H + OH -- DE → ABCDE + H20
Anabolism
synthesis of new molecules within body cells that uses energy
-- C + D + energy → CD
Exchange Reaction
involves decomposition of first, then synthesis
-- AB + CD → AD + CB
Reversible Reaction
occurs simultaneously in both directions
AB <-> A + B
@ equilibrium the amount of chemicals does not change even though the reactions are still occurring
Reversible reactions seek equilibrium
Enzymes
protein catalysts that lower the activation energy of reactions
not changed or used up in a reaction
Activation energy
amount of energy needed to get a reaction started
chemical reactions in cells cannot start without help
Exergonic (exothermic) reactions
produce more energy than they use
generates body heat
Endergonic (endothermic) reactions
use more energy than they produce
uses body heat
solution
mixture of 2 or more substances
solvent
medium (liquid, air)
solute
atoms, ions, or molecules which are dispersed (or dissolved) in solvent
solubility
water’s ability to dissolve a solute in a solvent to make a solution
ionization (dissociation)
ionic bonds broken in water due to polarity of water
hydration sphere
sheath of water molecules around an ion in solution
hydrophilic
water loving
molecules that interact readily with water molecules
ions, polar molecules
H+
extremely reactive in solution
pH
concentration of hydrogen ions (H+) in solution
concentration
the amount of solute in a solvent (mg/mL)
Neutral pH
balance of H+ and OH-
-pH of human blood -- from 7.35 to 7.45
Acidic
pH lower than 7.0
high H+ concentration
Basic (alkaline)
pH higher than 7.0
low H+ concentration
pH scale
inverse relationship with [H+]
ranged from 0-14
acid
a solute that dissociates in solution & releases H+
proton donor
strong acids dissociates completely in solution (HCI)
HCI → H+ Cl-
Base
a solute that removes hydrogen ions from a solution
proton acceptor
strong bases dissociate completely in solution (NaOH)
NaOH → Na+ OH-
weak acids & weak bases
fail to dissociate completely (carbonic acid → bicarbonate)
H2CO3 → H+ + HCO3
help balance the pH
salts
solution that dissociate into cations and anions (except hydrogen ions and hydroxide ions)
NaCl → Na+ + Cl-
buffers
stabilize pH by removing or replacing H+
neutralizes either a strong acid or strong base
sodium bicarbonate is very important in humans
buffers carbonic acid
antacids
a basic compound that neutralizes acid and forms a salt
tums, rolaids
inorganic compounds
molecules not based on carbon or hydrogen
oxygen, water, inorganic acids, bases and salts, carbon dioxide
usually small and structurally simple
organic compounds
molecules based on carbon or hydrogen
carbohydrates, proteins, lipids, nucleic acids
functional group
an arrangement of atoms in an organic molecule that is responsible for most of the chemical properties of that molecule
organic molecules
contain H, C and usually O
covalently bonded
contain functional groups that determine chemistry
macromolecules
polymers consisting of many small repeating molecules called monomers
monomers join by dehydration synthesis reactions
carbohydrates
contain C, H, O in a 1:2:1 ratio
monosaccharides
simple sugars with 3 to 7 carbon atoms
disaccharides
two simple sugars condensed by dehydration synthesis
polysaccharides (starches)
many monosaccharides condensed by dehydration synthesis
hydrolysis breaks disaccharides → monosaccharides
structure of glucose
(picture)
structure of polysaccharide glycogen
(picture)
lipids
carbon: hydrogen ration is 1:2
contain much less O than carbs
nonpolar & insoluble in water
hydrophobic molecules: fats, oils, waxes
need transporter in blood
fatty acids, eicosanoids, glycerides, steroids, phospholipids, glycolipids
primary components of cell membranes
simple lipids
fats or triglycerides
contain glycerol and fatty acids
formed by dehydration synthesis
broken by hydrolysis
chains of hydrocarbons
saturated
with hydrogen (no double bonds)
Unsaturated
( one or more double bonds between carbons)
complex lipids
contains C, H, and O & P, N, or S
phospholipids that make up membranes
hydrophilic
water loving
interacts with water
ions and polar molecules
hydrophobic
water fearing
does not interact with water
nonpolar molecules, fats, oils
steroids
four carbon rings with OH- group attached to one ring
part of membranes; keeps membranes fluid
proteins
most abundant and important organic molecules
contains C, H, O, N
20 amino acids - building blocks
amino acid structure
central carbon atom
hydrogen atom
amino group (--NH2)
carboxylic acid group (--COOH)
variable side chain or R group
amino acids
exist in either of two stereoisomers: D or L
L- forms are most often found in nature
connecting amino acids
requires dehydration synthesis between amino group and carboxylic group producing a peptide bond
7 major protein functions
support- structural proteins
movement- contractile proteins
transport- transport (carrier) proteins
buffering- regulation of pH
metabolic regulation- enzymes
coordination and control- hormones
defense- antibodies
protein structure
conjugated proteins- consists of amino acids combined with other organic molecules
glycoproteins
nucleoproteins
lipoproteins
primary structure
the sequence of amino acids along a polypeptide
secondary structure
hydrogen bonds form spirals or pleats
tertiary structure
secondary structure folds into a unique shape
quaternary structure
final protein shape - several tertiary structures together
denaturation
change in structure
due to temp, pH changes
protein becomes nonfunctional
fibrous proteins
extended sheets or strands
globular proteins
soluble spheres with active functions
protein function based on shape
shape based on sequence of amino acids
denaturation
proteins can undergo this
occurs when proteins encounter hostile environments such as temperature and pH
causes proteins to lose their shapes and functions
nucleic acids
large organic molecules found in nucleus
store & process information at molecular level
deoxyribonucleic acid (DNA)
determines inherited characteristics
directs protein synthesis
controls enzyme production
controls metabolism
ribonucleic acid (RNA)
controls and performs intermediate steps in protein synthesis
nucleotides
building blocks of DNA, RNA
3 molecular parts:
sugar (deoxyribose or ribose)
phosphate groups
nitrogenous base
(A, G, T, C, or U)
DNA
double stranded
bases form hydrogen bonds to hold together
twisting double- helix
purines pair with pyrimidines
adenine (A) to thymine (T)
cytosine (C) to guanine (G)
RNA
usually single stranded
uracil (U) replaces thymine; binds to adenine
messenger RNA (mRNA), transfer RNA (tRNA), ribosomal RNA (rRNA)
high energy compounds
nucleotides can be used to store energy
adenosine diphosphate (ADP)
two phosphate groups; di- = 2
adenosine triphosphate (ATP)
3 phosphate groups; tri- = 3