Organic Chem Carbohydrates
Org. chem
Study of compounds containing carbon
Carbohydrates
Lipids
Proteins
Nucleic acids
Functional groups
Hydroxyl
Methyl
Carboxyl
Amino
Phosphate
Monomers and polymers
Macromolecules: large organic molecules with high molecular weights
Most are polymers
Molecules made of a repetitive series of monomers
Formed by polymerization- joining of monomers
Dehydration synthesis
Hydroxyl group removed from a monomer and a hydrogen group is removed from another water is a by product
Anabolic reaction
Hydrolysis
Opposite of dehydration synthesis
Splitting of polymer into monomers with the addition of water
Carbohydrates
Hydrophilic organic molecules
2:1 ratio of hydrogen to oxygen
Ex: sugars and starches
Monosaccharides- simplest carbohydrates
Monomers of larger carbohydrates
Glucose
Blood sugar
Galactose
Fructose
All isomers of each other
Disaccharides
Sugars made of 2 covalently bonded monosaccharides
Sucrose
Table sugar
Glucose + fructose
Lactose
Milk sugar
Glucose + galactose
Lactose intolerant lack the enzyme that breaks down the lactose
Maltose
Sugar in grain products
Glucose + glucose
Oligosaccharides: short chains of 3 or more monosaccharides
Polysaccharides
Long chains of monosaccharides 50+
Glycogen
Energy storage in cells of liver, muscle, brain, uterus, vagina
Starch
Energy storage in plants that is digestible by humans
Cellulose
Structural molecule in plants that is important for human dietary fiber (indigestible)
Functions
Quickly mobilized source of energy
Oxidized to make ATP
Often bound to lipids and proteins
Glycoproteins and glycolipids have glucose attached to the lipids or proteins
Proteoglycans: more carbohydrate than protein
Lipids
Hydrophobic organ molecules with a high ratio of hydrogen to oxygen
More calories that carbohydrates
Not as easily metabolized
Fatty acids
Chains of 2-24 carbon atoms with carboxyl on one end and methyl on the other
Essential fatty acid: Must be obtained from food
Saturated
Carbon linked by single covalent bonds saturated with hydrogen
Unsaturated
Contain some double bonds
Polyunsaturated fatty acids: have multiple double bonds between carbons
Triglycerides
3 fatty acids linked to glycerol
Formed by dehydration synthesis/broken down by hydrolysis
Function: energy storage, insulation, shock absorption
Neutral fats: once stored no longer acidic
Oils: liquid at room temp
Ex: corn and olive oils
Saturated fats are solid at room temp
Animal fat
Trans fats
Triglyceride with more than one trans fatty acid
Isn't broke down easily
Vegetable shortening
Resist enzymatic breakdown
Raises risk of heart disease
Phospholipids
Triglyceride with one fatty acid replaced by a phosphate group
Amphipathic
Fatty acid tails are hydrophobic
Phosphate head is hydrophilic
Structural foundation of cell membrane
Eicosanoids
20 carbon compound derived from a fatty acid
Steroids
Lipid with 17 carbon atoms and 4 rings
Cholesterol is the parent steroid
Important for nervous system function and integrity of cell membrane
85% is internally synthesized in liver
15% comes from diet
Ex: testosterone
HDL= good cholesterol
LDL= bad cholesterol
High ratio of lipid to protein
Proteins
Polymer of amino acids
Amino group
R group
Carboxyl group
Peptide: composed of 2+ amino acids joined by peptide bonds
Peptide bond
Joins amino acid to carboxyl group
Dehydration synthesis
Named for the number of amino acids
Dipeptides: 2 amino acids
Tripeptides: 3 amino acids
Oligopeptides fewer than 10-15 amino acids
Polypeptides 15+ amino acids
3D shape
Conformation
Crucial to function
Denaturation: extreme conformational change that destroys function
Extreme heat of pH may cause permanent denaturation
Levels of complexity
Primary structure
Organization of amino acids
Recipe for DNA
Secondary structure
Coiled alpha helix
Fold beta sheet
Tertiary Structure
Globular proteins
Cell membranes
Enzymes
Fibrous protein
Muscle contraction
Need to withstand force
Quaternary structure
Only in some proteins
Hemoglobin
2+ polypeptide chains due to ionic bonds and hydrophobic
Functions
Membrane transport
Catalysis
Recognition and protection
Movement
Cell adhesion
Protein bind cells together
Enzymes
Proteins that function as biological catalysts
Some are ribozymes
Composed of RNA
Can act on more than 1 substrate
Speed up chemical reactions
Lower activation energy and speed up reactions
Reaction Rates
Concentration
Temperature
Higher temp.
Reactant properties
Smaller particles
Prescence of a catalyst
Named with -ase
Can be reused
How an Enzyme is used
Substrate binds to active site
Enzyme substrate specificity
Forms enzyme substrate complex
Enzyme releases reaction products
Enzymes can be altered
pH and temperature
Alter shape
Vary in optimum pH
Cofactors
Nonprotein partner to enzymes
Organic or inorganic
Organic: iron, copper, zinc, magnesium
Also called coenzymes
Vitamins
ATP, Nucleotides, nucleic acids
Nucleotides
Organic compound made of
Nitrogenous base
Sugar
1+ phosphate groups
Ex: ATP
Adenosine triphosphate
ATP
Body's most important energy transfer molecule
Stores energy from exergonic reactions
Holds energy in covalent bonds between phosphate
Energy transfers to and from ATP involve adding or removing the 3rd phosphate group
Hydrolysis of ATP is catalyzed by adenosine triphosphatases
Breaks 3rd phosphate bond to produce adenosine diphosphate
Phosphorylation
Done by energy kinases
GTP
Involved in energy transfer
cAMP
Formation is triggered by a hormone
2nd messenger within cell
DNA
Instructions for synthesizing proteins
RNA
