AP BIO unit 1

Foundation of Biology

The same valence and similar chemical properties

Hydrogen bonds , Attraction between + and - , Hydrophobic and hydrophilic interactions , Interactions with water

Covalent and Ionic

Pair of electrons shared equally by 2 atoms

Pair of electrons shared unequally by 2 atoms from differences in electronegativity

Low to High on periodic table

hydrogen bonds with each other

Cohesive and Adhesive Behavior, Moderation of Temperature, Expansion upon Freezing, Solvent

Upward movement of water in plants, built of Cohesion and Adhesion

binding of like molecules

binding of unlike molecules

as liquid evaporates, remaining surface cools like sweating

hydrogen bonds are more ordered and spread out

water loving

water fearing

hydrogen ions (H+), the more H+ the more acidic

acidic

neutral , pH of blood

basic (alkaline)

Carbon

combination of C & H (nonpolar and stable)

molecules with same molecular formula but different structure

Structural isomers, Geometric isomers, Enantiomers

Carbohydrates, Lipids, Proteins, Nucleic acids

long molecule consisting of many similar building blocks

small molecular building blocks with covalent bonds

occurs when two monomers bond together through the loss of a water molecule

proteins that speed up the rate of chemical reactions

water is added to break down polymers into monomers

break

include sugars and the polymers of sugars

simple sugars

many sugar building blocks

formed when a dehydration reaction joins two monosaccharides

storage polysaccharide of plants

storage polysaccharide in animals

structural, major component of the tough plant cell wall

structural, found in the exoskeleton of arthropods

Hydrophobic Fats, Steroids, and Phospholipids

stores energy, glycerol + 3 fatty acids = triglyceride

two fatty acids and a phosphate group are attached to glycerol

carbon skeleton consisting of four fused rings

Transport, Communication, Storage, Support

contain carboxyl and amino groups, linked by peptide bonds

polymers built from the same set of 20 amino acids

Primary, Secondary, Tertiary, Quaternary

the sequence of amino acids in a protein

the coiling and folding of the amino acid chain

determined by interactions between R groups (twists and turns)

results when two or more Tertiary structures form one functional macromolecule (outside layer formed)

Loss of proteins native structure

proteins that assist proper folding of other proteins, consists of hollow cylinder with a cap

Deoxyribonucleic acid (DNA), Ribonucleic acid (RNA)

two polynucleotides spiraling around an imaginary axis running from 5’ to 3’ in opposite directions

Adenine, Thymine, Cytosine, Guanine

A and G (2 rings)

C, T, U (1 ring)

A&T , C&G

different covalent arrangements of atoms

same covalent arrangement of atoms but different spatial arrangements

mirror images of eachother

have the maximum number of hydrogen atoms possible and no double bonds

have one or more double bonds

Tails = hydrophobic, Phosphate group head = hydrophilic