Covalent Bonds
Sharing of valance electrons by 2 atoms
Strongest bond
form molecules in cell
Single Cov → sharing 1 pair of electrons
Double Cov → sharing 2 pairs of electrons
Polar & Non-polar Cov Bonds
Polar Covalent Bonds
Unequal sharing of electrons in the cov. bond
Electronegative Atom
Has a strong pull on electrons
Non-Polar Covalent Bond
Equal sharing of electrons in cov. bond
Ionic Bond
Transfer of electrons from 1 atom to another → causes both atoms to have a charge
Cation
Pos Atom in ionic bond
Anion
Neg Atom in Ionic bond
Ion
Just a charged atom
Weaker Bonds
reenforce shape of large molecules
help molecules adhere to each other
allow for temporary interactions
Hydrogen Bonds
form when H is cov. bonded to one atom and then is also attracted to another electroneg. atom
ex: H on H20 is attracted to O on another H2o molecule
Water
all living orgs. need water
cell = 70-95% water
water is a polar molecule
able to h-bond with other polar molecules
4 emergent properties of water:
Cohesion & Adhesion
Temp Moderation
Expansion Upon Freezing
Versatility as a solvent
Cohesion & Adhesion
Cohesion: H2O molecules stick to each other thru h-bonding
Adhesion: H2O molecules sticking to other polar molecules thru h-bonding
Both contribute to surface tension
Surface Tension
how hard it is to break the surface of a liquid
Connect to cohesion and adhesion
Temp. Moderation
water has a ^ specific heat
measure of how well a substance resists a change in temp (when it absorbs/ releases heat)
water resists a change in it’s temp
ex: biological relevance: bodies of water have stable temps
allows for the health of species that live there
milder climate
Expansion upon Freezing
ice is ~10% less dense than water
ice floats on top of water
as liquid, water’s h-bonds are irregular/unstable
as solid, water’s h-bonds are stable/organized so h2o expands as it freezes
Versatile Solvent
like dissolves like
H20 is polar
water can dissolve other polar substances
Hydrophillic
water-loving
affinity for H2O
polar/charged particles/molecules, sodium chloride
Hydrophobic
water fearing
repels water
ex: non-polar, non-ionic
Oil
pH scale
relative concentration of H ions
Acids < 7, excess of H
Bases > 7, excess of OH
Neutral = 7
Physiological pH
7.4
Carbon Chem/ Orgo
Carbon can form macromolecules
Tetravalent
Major partners = (C, H, O, N)
Macromolecules
diverse, large, and complex molecules
C forms
Carbs
Nucleic Acids
Protein
lipids
Tetravalent
4 valance electrons
can form 4 cov. bonds
ex: C
Hydrocarbons
non-polar, hydrophobic
molecules made up of H & C
in living things, in lipids
Functional Groups
6 groups
components of macromolecule involved in chemical rxns
ex: phosphate
Polymer
large molecules composed of building blocks called monomers
3 macromolecules are polymers
Monomer
cov. linked to form polymers
Synthesis
to make something
Dehydration Synthesis
allows the formation of polymers
h20 is taken away & a new cov. bond is left in its place
how monomers are added to make polymers
Hydrolysis Rxns
reverse of dehydration synthesis
breaking w/ water
breaking apart polymers into monomers
h20 is added, breaks cov. bond b/w monomer & polymer chain
Carbs
monomers = monosaccharides
molecular formula is usually multiple of CH2O
Sugars -ose
2 monosaccharides → disaccharides
covalent bond = glycosidic linkage
b/w two monosaccs.
3 or more monosaccs. → produces polysaccharides
Monosaccharides
Monomers of Carbs
Disaccharides
2 or more monosaccharides
Polysaccharides
3 or more monosaccharides
Glycogen
Chitin
Starch
Cellulose
Glycosidic Linkage
Covalent bond between monosaccharides
Glycogen
Animal: Energy Storage
helical shape
stored in liver & muscles
Chitin
Animal: Structural
linear shape
exoskeleton of arthropods
ex: surgical thread
Starch
Plant: enegry storage
helical shape
store starch in chloroplasts
*plants access energy by breaking down starch
Cellulose
Plant Structure
linear
straight form string building material
major compound of plant cells
Proteins
macromolecules
have diverse fxns
do all jobs in the cell
Made of amino acids and polypeptides
Amino Acids
monomer of proteins
20 types
Polypeptide
polymer of protein
Peptide Bond
cov. bond b/w monomers
R group
part of the a.a that is different from 1 a.a to another
connected to main carbon
Primary Structure
sequence of a.a monomers
held together by peptide bonds (strong bonds)
Secondary Structure
coils and folds in the polypeptide
result from h-bonding
Tertiary Structure
caused by interactions b/w R groups of the a.a’s
Every protein has tertiary, secondary, and primary structure
Quaternary Structure
only found in proteins made of multiple polypeptides
2 or more polypeptides
Denaturation
loss of protein shape ( 2nd, 3rd, & 4th structure)
denatured protein = biologically inactive ( loses function)
1st structure is not effected b/c it is held together by cov. bonds
Causes:
extreme pH
high temps
high salinity
Renaturation
protein gaining shape & function again
Nucleic Acids
DNA & RNA
RNA
ribonucleic acid
Monomers: A, G, C, U
Sugar: Ribose
DNA
Deoxyribonucleic acid
genetic code
directs the synthesis of proteins
Letters: A, G, C, T
Pentose: deoxyribose
Nucleotide
Monomer of nucleic acids
Polynucleotide
Polymer of nucleic acids
Phosphodiester Linkage
Cov. bond b/w monomers
Lipids
do not form polymers
mainly hydrocarbons
most important:
fats
phospholipids
steroids
Fats (Triglycerides/triglycerals)
3-carbon molecule w/ hydroxyl group attached to each carbon
3 fatty acids = carboxyl group + hydrocarbon (16-18 carbons)
fatty acids attached to glycerol thru dehydration syn.
major function = energy storage
Sat & UnSat
Phospholipids
Phosphate -
made up pf glycerol + 2 F.A + 1 P
F.A = hydrophobic
P = hydrophilic
Steroids
carbon stack w/ 4 fused rings and functional groups attached
Ester Linkage
Cov. bond b/w lipids
Saturated Fats
saturated w/ H
no double bonds b/w carbon
solid at room temp
animal fats
Unsaturated Fat
“unsaturated with H”
1 or more double bonds w/ carbon
oils
liquid at room temp
* double bond prevents tight packing of molecules
Metabolism
Metabolic Pathway
Catalyze
Catabolic
Anabolic
Non-Spontaneous
requires input of energy
cannot
Spontaneous
occur w/o input of energy
can be fast or slow
Free Energy (G)
potential energy that can do work in a cell
Change in G for a rxn = G final - G initial
Rxns w/ a - Change in G are spontaneous
rxns w/ a + change in G are non-spontaneous/anabolic/endergonic
Exergonic
- Change in free eneergy (G)
release G (used to do work in the cell)
Exergonic / Catabolic / Spontaneous
Endergonic
consume/ Use G
Store G in molecules
Endergonic / Non-Spontaneous / Anabolic
Mechanical Work
Physical change
Transport Work
Moving substances across membrane
Chemical Work
Ex: Synthesis of polymers
ATP
Energy molecules
Hydrolysis rxn breaks a p-p cov bod
G is released
products are ADP + P
Renewable resource
Energy Intermediate
stores potential energy
provides G for cellular work
Energy Coupling
exergonic process drives endergonic process