Dat Chemistry

Front 1

Types of Chemical bonds

Back 1

1) Ionic-----electrons are transfered

2) Covalent--- electrons are shared
***Nonpolar covalent ---shared equually
***Polar covalent----not equally shared

3) Hydrogen bonds --- weak bond due to dipole in 2 molecules

Front 2

Properties of water

Back 2

1)solvent --- great solvent for polar or ionc substances due to polarity

2) Hydrophobic---- water fearing, non polar
3) hydrophillic --- water loving polar

4) High heat capacity----- must add larg quanity of heat / energy to change temp of H2O

5) Ice Floats---- becomes less dence then liquid, latic / chrystal structure

6) Cohesion ----- sticks to its self hydrogen bonds, = high surface tension

7) Adhesion----stick to polar stuff,

Front 3

Organic molecules

Back 3

Made of Carbon and Hydrogen atoms

1)Macromolecules ----

2) Polymers----molecule sthat consits of a single unit (monomers) repeted many times

Front 4

Functional Groups

Back 4

1) Hydroxyl -OH
2) Carboxyl -COOH
3) Amino -NH2
4) Phosphate -PO3
5 Carboonyl -C=O (ketone)
6) Carbonyl -COH (Aldehydes)
7) methyl -CH3

Front 5

Carbohydrates

Back 5

1) Monosaccharide --- single sugar moleculelike fructose glucose

2) Disaccharide---2 sugar molecules joined by a glycosidic linkage (loss of H2O)

3) Sucrose = glucose + fructose

4)Lactose = glucose + galactose

5) maltose = glucose + glucose

6) Polysaccharide--- a series of connecteed monosaccharides. Starch, Glycogen, Cellulose, Chitin

Front 6

Lipids

Back 6

Lipids are insoluble in water but soluble in nonpolar substacnes

1) Triglycerides (triacylglycerols) ---Consist of 3 fatty acids attached to a glycerol molecule.

*** Saturated fatty acid has no doubble bonded carbons

***Monounsaturated fatty acid ahs one double bonded carbon

***polyunsaturated fattya acid has two or more double bonds

2) Phospholipid--- Just like lipid except one fatty acid chain is replaced w/ phosphate group
***Amphipathic ---Hydrophilic head and hydrophobic tail

3)Steroids--- back bone of 4 carbon rings, cholesterol testosterone estrogen

Front 7

Proteins

Back 7

All proteins are polymers of amino acids ie a chain of amino acids covalently bonded by peptide bonds and the chaiin is a poly peptide

Group by function

1)Structural proteins---- karatin in hair

2) Storage proteins ---- casein mild

3) Transport proteins --- cell membran

4) Defensive proteins --- Antibodies

5) Enzymes--- regulat chemical RXN

Structure of protein

1) primary structure --- describes the order of amino acids

2) Secondary structure--- 3D shape via H-bonding a-helix and B-pleated sheet (fibrous proteins)

3) Tertiary structure--- additional 3D shaping H-Bonding and ionic bonding between R groups and hydrophobic effect and disufide bonds (globular)

4) Quaternary structure--- protein that is assembled form two or more separate peptide chains like hemoglobin

Front 8

Nucleic Acids

Back 8

1) DNA (deoxyribonucleis acid) is a polymer of nucleotides

2) Nucleotide ----consists of 3 parts
***nitrogen base
***deoxyribose ( a suger)
***phosphate group

3) 4 nucleotides each w/different base
***Adenin --2 ring (purine)
***Thymine - 1 ring (pyrimidine)

***Cytosine 1 ring (pyrimidine)
***Guanine - 2 ring (purine)

RNA
1) sugar is ribose
2)NO thymine replaced by uracil
3)single strand

Front 9

Chemical RXN in Metabolic processes

Back 9

chemical reactons that occur in bio systems = metabolism
catabolism = breakdown
Anabolism (synthesis) = formation
Activation energy---energy needed to creat new bonds
Catalyst---accelerates the rate or RXN w/o beeing consumed

1) Equilibrum = rate of r forward rxn = rate of reverse rxn.
2)Enzymes - globular proteins that act as catalysts
***enzymes act on substrate
***Enzymes are substrete specific
***enzymes is unchanged as a result of a reaction
***enzyme catalyzes a RX both directions
***standerd suffix is "ase"
***Induced fit model describes how enzyems work

3)Cofactors --non protein molecule sthat assist enzyes
***coenzymes are organic cofactors vitamins
***inorgaic cofators metal ions

4) ATP (Adenosine triphosphate) common source of energy of activation ATP->ADP makes new bonds
ATP are assembled by phosphorylation ADP->ATP

Refulation of chmeicla RXN
1) Allosteric Enzymes --- two binding sites
***acitve site for substrate
***Allosteric effector---Activator / inhibitor

2) Competitive inhibition---mimics the substrate inhibits enzyme by occupying active site prevents enyme form catalyzing substrate

3)noncompetivive inhibiton --inhibits by binding to enzyme at a location other then the acivation site.

4) cooperativeity----- binding capacity increase after the 1st substrate binds to a acitve site in quaternary structure