Organic Chem
Introductory Information:
All of life is built on carbon
Cells are 72% H2O and 25% carbon compounds and 3% salt
Organic Chemistry is the study of carbon compounds
Polar → oppositely charged
Non-polar → equally charged and covalent bonds ( mutual sharing of one or more pairs of electrons between two atoms)
Hydrolysis Synthesis
Dehydration Synthesis
Types of structures:
Hydrocarbons: (non-polar),hydrophobic , and gas at room temperature
Isomers
Molecules with the same molecular formula and different structure
Diffrent chem properties
Diffrent biological functions
Form affects function
Structural différences create important functional significance
Functional Groups:
Parts of organic molecules that are involved in chemical reactions
Hydroxyl, amino, carbonyl, carboxyl, sulfydryl, phosphate
Prefixes and suffixes:
(Refer to knowt.io)
Meth 1
Eth 2
Prop 3
But 4
Pent 5
Hex 6
Hept 7
Oct 8
Non 9
Dec 10
Ane all single bonds
Ene at least one double
Yne at least one triple
Diversity of molecules:
Substitute other atoms or groups around the carbon
Gas vs liquid
Polar vs non polar
Biological effects
Hydroxyl
- OH (alcohols)
- Names typically end in OL
- EX: ethanol
Carbonyl
- O double bonded to C (C=O)
- If C=O to end molecule aldehyde
- C=O in the middle of molecule ketone
Carboxyl
- COOH
- C double bonded to O & single bonded to OH group
- Acids
Amino
- NH2
- Amono acids
- NH2 acts as bases
Sulfhydryl
- SH
- S bonded to H
- Compounds with SH=thiols
Phosphate
PO4
Lots of o+lots of neg charge
Highly reactive
Proteins
Introductory information:
Most structurally and functionally diverse group
Involved in primarily everything
Enzymes (pepsin and DNA polymerase)
Structure (keratin and collagen)
Carriers & transportation (hemoglobin and aquaporin)
Cell communication
- Signals (insulin and other hormones)
- Receptors
Denfesnse (antibodies)
Movement (actin and myosin)
Storage (bean seed proteins)
Structure:
Monomer = amino acids
Polymer = polypeptide
Peptide bond and a polypeptide chain
Amino acids -> central carbon, amino group, carboxyl group, R group
Non-polar:
(Non-polar and hydrophobic)
Glycine (Gly)
Alanine (Ala)
Valine (Val)
Polar:
(Polar and hydrophilic)
Serine (ser)
Cysteine (cys)
Histidine (his)
Peptide bonds:
covalent bond between NH2 (amine) of one amino acid
C — N bond
Primary 1* structure
Order of amino acids in chain
Amino acid sequence determined by gene (DNA)
Slight change in amino acid sequence and function
Secondary 2* structure
Local folding
Folding along short sections of polypeptide
Interactions amino acids
Forms of section 3-D structures
Tertiary 3* structure:
- Entire molecule folding
Quaternary 4* structure:
More than one polypeptide chain bonded together
Becomes functional protein
Hydrophobic
Carbohydrates
Functions:
- Comprises of C, H, O
- Provides energy, storage of energy, raw materials, and structural materials
- Monomer -> simple sugar (monosaccaride)
- Polymer -> polysaccharides, starch, glycogen
Building sugars:
- Dehydration synthesis
- Forms a glycosidic linkage
Cellulose:
Most abundant organic compound
100- 1,000 glucose monomers
Lipids
Structure:
- Dehydration synthesis
- Ester linkage is evident between OH&COOH
- Long HC chain
Purpose of fats:
Energy storage
Cushion organs
Insulates the body
Saturated fats:
All C bonded to H
No double carbon bonds
Long and straight
Animal fats and solid at room temp
Unsaturated Fats:
Primarily double bonds
Fish and veggie fats
Liquid at room temp
Phospholipds:
Tails are fatty acids -> hydrophobic (hide)
Heads are PO4 -> hydrophilic (attract)
Steroids:
different steroids are created by attaching different functional groups to rings
Different structures created different functions