Isomers -Molecules with the same molecular Formula

Structural Isomers -Molecules with the same molecular Formula but

different bond structures
Stereoisomers -Molecules with the same molecular Formula but
differ in how groups are attached
Enantiomers -Mirror image molecules (Chiral), D-sugars and L-
amino acids
Macromolecules, Dehydration and Hydrolysis -Monomer: Small, similar chemical subunits
-Polymer: Built by linking monomers
-Dehydration: Formation of large molecules by
removal of water (monomers are joined to form
polymers)
-Hydrolysis: Breakdown of large molecules by the
addition of water (polymers are broken down to
monomers).
Carbohydrates and examples -Molecules with a 1:2:1 ratio of carbon, hydrogen,
oxygen (CH2O)
-C-H covalent bonds hold much energy
(carbohydrates are good energy storage
molecules)
-Examples: Sugars, starch, glucose
Monosaccharides, isomers, enzymes role -Simplest Carbohydrate (Glucose C6H12O6)
-Fructose is a structural isomer of glucose
-Galactose is a stereoisomer of glucose
-Enzymes that act on different sugars can
distinguish structural and stereoisomers of
skeleton
Dissacharides and examples -2 monosaccharides linked together by dehyfration
synthesis
-used for sugar transport or energy storage
-examples: sucrose, lactose, maltose
Polysaccharide and examples -Long chains of monosaccharides (linked through
dehydration synthesis)
-Energy Storage: Plants use starch, animals use
Glycogen
-Structural Support: Plants use cellulose,
anthropods and fungi use chitin
Nucleic Acids, sugar and nitrogenous base -Monomer: Nucleotides (nucleotides connected by
phosphodiester bonds to form polymer)
-Polymer: Nucleic Acids
-Composed of: Sugar + Phosphate+ Nitrogenous
base
-Sugar is deoxyribose in DNA (addition of H atom)
and ribose in RNA (addition of OH)
Nitrogenous bases include: Purines (adenine and
Guanine) and Pyrimidines (Thymine, Cytosine,
Uracil)
Deoxyribonucleic Acid (DNA) -Encodes information for amino acid sequence of
proteins (sequence of bases)
-Double helix: 2 polynucleotide strands connected
by hydrogen bonds (2 strands)
-Base Pairing rules: A with T (or U in RNA), C with G
-Sugar-phosphate backbone
Ribonucleic Acid (RNA) -RNA similar to DNA except: contains ribose
instead of deoxyribose, and contains uracil instead
of thymine
-Single Polynucleotide strand
-RNA uses information in DNA to specify sequence
of amino acids in proteins
-Ribose-phosphate backbone
7 Functions of Proteins 1. Enzyme catalyst
2. Defense
3. Transport
4. Support
5. Motion
6. Regulation
7. Storage
Amino Acids and Proteins -Proteins are polymers: composed of or more
long, unbranched chains (each chain is a
polypeptide)
-Amino Acids are monomers composed of: Central
carbon atom, amino group, carbonyl group, single
hydrogen, variable R group.
-Amino Acids are joined by dehydration synthesis
(creates a peptide bond)
Proteins 4 Levels of structure -The shape of a protein determines its function
1. Primary Structure- Sequence of amino acids
2. Secondary Structure- Interation of groups in the
peptide backbone (alpha helix=circular), (beta
sheet= pleated sheet)
3. Tertiary Structure- Final folded shaped of a
globular protein.
-stabalized by a number of forces
-final level of structure for proteins consisting of
only a single polypeptide chain.
4. Quaternary Structure- Arrangement of
individual chains (subunits) in a protein with 2 or
more polypeptide chains.
Additional Structural Characteristics of Proteins -Motifs: Common elements of secondary structure
seen in many polypeptides. Useful in determining
the function of unknown proteins
Domains: Functional units within a larger
structure. proteins made of multiple domains that
perform different parts of the proteins functions
Chaperones -Chaperon proteins help protein fold correctly
-Deficiencies in chaperone proteins implicated in
certain diseases. (Cystic Fibrosis is a hereditary
disorder, from incorrectly folded proteins)
Denaturation -Protein loses structure and function
-Due to environmental conditions (pH,
temperature, ionic concentration of solution)
Lipids and Examples -Loosely defined group of molecules with one main
chemical characteristic (insoluble in water)
-High Proportion of nonpolar C-H bonds causes the
molecule to be hydrophobic
-Examples: Fats, oils, waxes, and even some
vitamins
Fats (Tryglycerides, Fatty Acids) -Triglycerides: composed of 1 glycerol and 3 fatty
acids
-Fatty Acids: Need not be identical, chain length
varies
saturated- no double bonds between carbon
atoms (high melting point)
Unsaturated- 1 or more double bonds (low
melting point)
Trans fats: produced industrially
Phospholipids Composed of: Glycerol, 2 fatty acids (nonpolar
tails), and a phosphate group (polar head)
-Forms all biological membranes
Micelles -Lipid molecules orient with polar (hydrophilic)
head toward water and nonpolar (hydrophobic)
tails away from water.
Phospholipid Bilayer 2 structures form.
-Hydrophilic head points outward
-Hydrophobic tails point inward toward each other