BIO CHEMISTRY
MACROMOLECULES
CARBOHYDRATES
COMPLEX
POLYSACCHARIDES
Long chains of monosaccharides linked by glycosidic bonds
Starch
Straight chain
Alpha bonds
Cellulose
Branched chain
Beta bonds
POLYMERIZATION
Process of small molecules, called monomers chemically combine to produce a large chainlike molecule called polymers
Polymers
SIMPLE
MONOSACCHARIDE
SINGLE SUGAR UNIT
Glucose
Energy source
1:2:1 ratio of C, H, O
Two types of glucose
A glucose
OH functional group: bottom
B glucose
OH functional group: top
Fructose
Sugar in fruit
Galactose
Sugar in yogurt
ISOMERS
Glucose, Fructose, Galactose
Molecules with the same chemical formula but different arrangement of atoms
C6H12O6
Monomers
DISACCHARIDES
TWO SUGAR UNITS
Lactose
Sugar found in milk
Glucose + Galactose
Sucrose
Table sugar
Glucose + Fructose
Maltose
Malt sugar
Glucose + Glucose
LINKAGE
Glycosidic bond
Bond between two monosaccharides
Alpha glycosidic bond
OH functional group is on same side of each monomer
Beta glycosidic bond
OH functional group is on opposite sides with respect to its neighbor on each monomer
Main energy source for organisms
Sugars are broken down to release energy (ATP)
Carbohydrates end in -ose
Composed of: O, H, C atoms
Polar
Soluble in water
FUNCTIONS
Source of energy
Glucose
Storage
Starch: Plant roots
Structural
Plants: Cellulose (Plant cell wall)
LIPIDS
FUNCTIONS
Long term energy storage
Protect and cushion organs
Dissolve fat soluble substances
TYPES
TRIGLYCERIDES (FATS)
STRUCTURE
Glycerol + 3 fatty acid chains
Joined together by ester linkage
ESTER LINK
-COO-
Fatty acid chains
Carboxyl functional group at one end
Hydrocarbon chain in the middle
Methyl group at other end
SATURATION
Unsaturated
Contains double bonds
The healthier fat
Oils
Plant source
Liquid at room temp
Saturated
Contains single bonds
The unhealthier fat
Solid at room temp
Butter
Animal source
PHOSPHOLIPIDS
STRUCTURE
Glycerol + 2 fatty acid chains + phosphate group
HYDROPHILIC
Contains hydrophilic head: Phosphate group (Likes water)
HYDROPHOBIC
Contains hydrophobic tail: fatty acid chain (Repels water)
Structural component of cell membranes
STEROIDS
Formed by 4 fused rings
Functional groups on ring change steroids molecule type
Cholestrol
Testosterone
Estrogen
Progesterone
WAXES
STRUCTURE
Alcohol chain + Fatty acid chain
PROPERTIES
Hydrophobic, non polar
Protective compounds: waterproof barrier
Animals
Plants
PROTEINS
Monomer
AMINO ACID
Every protein consists of 20 amino acid monomers arranged in different ways.
"Essential" 8 amino acids
STRUCTURE
Amino acid group: -NH2
R group
The R group is responsible for determining the characteristics of the amino acids. What differentiates them
Carboxyl group
Polymer
Proteins are polymers of amino acids
LINKAGES
Proteins are formed by two amino acids linked together by peptide bonds
Peptide bond: "C-N"
Polypeptide bond: linking many amino acid chains
4 PROTEIN STRUCTURES
PRIMARY
Sequence of amino acids in polypeptide chain
SECONDARY
Hydrogen bonds form between amino acids
A helix: spiral shape
B pleated: sheet shape
TERTIARY
More bonds form between functional groups
Coiled/foiled further
Often complete and works
More complex 3D structure
QUATERNARY
Two or more tertiary structures bind
Hemoglobin
Held together by polypeptide bonds
Proteins are only functional when polypeptide folding into correct 3D shape
DENATURATION
Process where protein unfolds, leading to functional and structural loss
CAUSES
PH
Temperature
4 MAIN FUNCTIONS
STRUCTURE: supports tissue
ENZYMES: speed up reactions
TRANSPORT: moves substances in and out
CHEMICAL MESSENGER: sends signals
ENZYMES
CATALYST
Makes reactions occur where they typically wouldn't
Not used up in reaction
ORGANISMS INVOLVED: ENZYME CYCLE
ACTIVE SITE
Groove in an enzyme that a substrate binds to
SUBSTRATE
Substance that binds to the active site of an enzyme
ON AND OFF SWITCH
ACTIVATOR: ON
INHIBITOR: OFF
NON COMPETITIVE
Substrate is still able to bind. Reaction is blocked
COMPETETIVE
Substrate competes with inhibitor to bind to active site. Active site is blocked, cannot bind.
FEEDBACK INHIBITION
Activity of enzyme is inhibited by the end product binded to the beginning of the pathway
Reduces the waste of cellular resources
STRUCTURE
INDUCED FIT MODEL
Active site changes shape to fit substrate
LOCK AND KEY MODEL
Substrate fits perfectly into active site
FACTORS AFFECTING ENZYME ACTIVITY
TEMPERATURE
TOO HIGH
TOO LOW
Insufficient activity
Denatured
PH
TOO HIGH
TOO LOW
Denatured
PROSTHETIC GROUP
Non protein organisms that assist catalyst reactions
CO FACTOR
Helps activate enzymes
Metal ions
CO ENZYME
Acts as carrier for chemical group
Vitamins
ALLESTORIC CITE
Binding site that is different to enzymes active site
ALLESTORIC MODULATOR
Controls activity of enzyme
Changes function of protein
Type of protein
"ase" ending
NUCLEIC ACIDS
Monomer
Nucleotides
DNA: Deoxyribose
LOCATION
Found in nucelus
PURPOSE
Genetic instructions to make RNA
NITROGENOUS BASES
A, T, G, C
Double stranded
RNA: Ribose
PURPOSE
Converts DNA instructions to make proteins
LOCATION
Found in nucelus, and cytoplasm
NITROGENOUS BASES
A, U, G, C
Single stranded
Polymer
FUNCTION
Store genetic information
STRUCTURE
Pentose sugar
Phosphate group
Nitrogeous base
Ribose, deoxyribose
LINKAGE
Phosphodiester bond
Bond linking 2 sugars of a nucleic acid
BONDS AND REACTIONS
DEHYDRATION SYNTHESIS
Combines two molecules into a single molecule, with the loss of water
NEUTRALIZATION
Acid+Base react to form Water+Salt. H+ and OH- ions are involved.
REDOX
The transfer of electrons between two reactants
HYDROLOSIS
A larger molecule breaks to form smaller molecules, involves adding a water molecule
INTERMOLECULAR FORCES
HYDROGEN BONDS
Strong intermolecular force where a hydrogen (H) atom covalently bonded to N, O, or F interacts with another N, O, or F.
VAN DER WAALS FORCE
Weak, temporary attractions between molecules due to instantaneous dipoles.
DEFINITION
Forces of attraction between molecules (not within).
INTRAMOLECULAR FORCES
COVALENT
Formed when electrons are shared between atoms
POLAR COVALENT
A type of covalent bond where electrons are shared unequally, creating partial charges (δ+ and δ−).
IONIC
Formed when electrons are transferred from one atom to another.
MEMBRANE STRUCTURES
FUNCTIONS OF PLASMA MEMBRANE ORGANISMS
RECEPTOR PROTEINS
Bind to external chemicals to regulate processes in cell
RECOGNITION PROTEINS
Provide fingerprint for cells, to be recognized by other cells
CARBOHYDRATE CHAIN
CHOLESTROL
Helps membrane maintain flexibility
TRANSPORT PROTEINS
Provides passage way for molecules to go in and out of cell
ENZYMATIC PROTEINS
Accelerate intracellular and extracellular reactions on plasma membrane
PHOSPHOLIPID ARRANGEMENT
Head: OUT
Tail: IN
Formation keeps molecules from passing through too easily
FLUID MOSIAC MODEL
FLUID
Phospholipids + Proteins are not rigid
Move freely like a liquid
MOSIAC
Membrane is made up of different molecules
Scattered like mosiac art
GENERAL CELL STRUCTURES
GOLGI BODY
Processes and packages lipids and proteins to go IN and OUT of cell
MITOCHONDRION
Breaks down glucose, produces atp, powerhouse of cell
NUCLEUS
Stores genetic info (DNA)
NUCLEOLUS
Made of RNA
Produces ribosomes, helps with protein creation
NUCLEAR ENVELOPE
Double membrane structure, separates nucleus from cytoplasm
ENDOPLASMIC RETICULUM
ROUGH ER
Contains ribosomes
Protein synthesis + folding (assembly of proteins)
SMOOTH ER
No ribosomes
Synthesises + concentrates lipids, detoxifies chemicals
VESICLE
Membrane bound sacs
Carries proteins + lipids from ER to golgi, then to other parts
TEMPORARY
VACUOLE
Food storage of cell
Stores waste
PERMANENT
CELL WALL
Provides structural strength + support
PLASMA MEMBRANE
Surrounds cytosol of cell + dynamic barrier
LYSOSOME
Contains digestive enzymes, waste disposal
CYTOPLASM
Fluid substance in cell, except nucelus
PLASTID
Photosynthesises + storage in plants
CHLOROPLASTS
Enzymes + Pigments
AMY LAST
Stores starch
CHROMOPLASTS
Makes + stores pigment
Plant cells
ORGANELLE
Internal functional structure within cytosol
ENDOMEMBRANE SYSTEM
Packages, modifies, and transports proteins and lipids
ORGANELLES INVOLVED
Nucleus
Smooth ER, rough ER
Vesicle
Golgi body
Plasma membrane
TONCICTY
What occurs to cells immersed in external solution
DIFFUSION
Movement of particles from a high to a low concentration
PASSIVE
Osmosis
Diffusion of water particles across a semi permable membrane
SEMI PERMABLE MEMBRANE
Membrane that allows some molecules through but not others
Along gradient: HIGH to LOW
Doesn't require energy (ATP)
ACTIVE
Against gradient: LOW to HGIH
Requires energy (ATP)
BULK TRANSPORT
ENDOCYTOSIS
Brings materials IN
EXOCYTOSIS
Brings materials OUT
FACILITATED DIFFUSION
Transport of molecules across plasma membrane with help of transport molecules
CHANNEL PROTEIN
Opens in centre like a gate
Transports ions: H+, Ca+
CARRIER PROTEIN
Changes shape to let molecules pass through
Transports molecules: amino, sugars
TYPES OF SOLUTION
HYPERTONIC
More water INSIDE, more solute OUTSIDE
Water flows OUT
Cell SHRINKS
Animal cell: crenate (shrinks)
Plant cell: plasmolysis
ISOTONIC
HYPOTONIC
More water OUTSIDE, more solute INSIDE
Water flows IN
Cell EXPANDS
Animal cell: lyse (rupture)
Plant cell: comfortable (turgid)
FACTORS AFFECTING SOLUTES
Size: small molecules flow easier
Charge: Neutral molecules flow easier
Distance: smaller cell = faster diffusion
Concentration gradient: easier to go from high to low
EQUILLIBRIUM
Equal amount of water on both sides of membrane