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Carbohydrates:

• Sugars and their Molecules


• Monosaccharide, disaccharides, and polysaccharides
○ Monosaccharides:
 Multiple of CH2O
 Carbonyl group and hydroxyl group
 Carbon skeleton length: 3-7
 Different arrangements around asymmetric carbon
 Ex. Glucose vs. galactose
○ Dissacharides:
 Polymer of sugars
 Storage and structural roles
 Macromolecules of many monomers linked by glycosidic linkages.
 Starch: Helical, storage polysaccharide in plants made of only glucose
monomers with some branches.
• Plants store them in plastids (issued by hydrolysis)
• Animals store them in glycogen (issued by hydrolysis)
 Cellulose: Structural polysaccharide used in cell walls of plants.
• Microfibrils: Made by binded cellulose which cannot be digested
—good for digestive system?
• Some microbes can hydrolyze cellulose (Ex. Bacteria in cow,
termites).
 Chitin: Exoskeleton material in insects, etc. Hard because of calcium
carbonate. Cell wall function in fungi.

Lipids:
• Made of Glycerol (alcohol with 3 carbons and hydroxyl group at end) and Fatty Acid
(carboxyl group with hydrocarbon chain).
• Hydrophobic.
• Triaglycerol?
○ Composes fats and oils.
○ Bonded by ester linkage.
• Saturated Fatty Acid:
○ No double bonds
○ As many H as possible
○ Saturated Fats-solid in room temperature
• Unsaturated Fatty Acid:
○ At least one double bond
○ Not as many H as possible
○ Unsaturated Fats-Liquid in room temperature.
• Hydrogenate:
○ To add H synthetically to an unsaturated fat to make it solid in room temperature.
• Fat: Major energy storage (like gasoline)
○ Animals need fat because they move.
○ Stored in adipose cells
○ Cushion and insulation
• Phospholipids:
○ Like fats; two tails; structural differences.
○ Hydrocarbon tail
○ Hydrophilic head
○ Assemble with tail inside:
 Micelle cluster
 Phospholipid bilayer
• Found in plasma membrane
• Steroids:
○ Lipids with four fused rings on carbon skeleton
○ Vary with functional group on rings
○ Ex. Cholesterol:
 A steroid found in animal membranes and precursor from which steroids
are made.

Proteins:
• Purposes of Protein: Support, storage, transport, signaling, movement, defense against
foreign substances, enzymes.
• Vary in 3-D structure
○ Most complex
○ Made of polymers from 20 amino acids-polypeptides.
• Definition: One or more polypeptide folded/coiled into specific conformations.
• Amino Acid:
○ Organic molecule
○ Asymmetric carbon center (alpha carbon)
○ For Parts:
 Amino Group
 Hydrogen Group
 Carboxyl Group
 R (variable) Group
• R property determines the type of amino acid.
• Ex. Nonpolar, polar, acidic (+), basic (-)
• Describes R, not other parts of amino acid.
• Peptide Bond:
○ Links two amino acids (carboxyl group next to amino group) by enzyme
(dehydration reaction).
○ Forms Polypeptide.
○ 1 End (free amino group): N- Terminus
○ Other end (carboxyl): C- Terminus
• Polypeptide Backbone:
○ Has different appendages/side chains
○ Vary in length
• Polypeptide Chains
○ A group that forms a functional protein.
○ The ability of a protein to recognize and bind to certain things determines its
purpose (it depends on molecular order and levels of structure.
○ Folds/conforms as it is synthesized by a cell
• Primary Structure:
○ A protein’s unique sequence of amino acids.
○ Ex. Lysozene has 129 amino acids chain.
○ The order is determined genetically, and an error can cause deformation/disease
 Ex. Sickle Cell
○ Sanger: Worked out amino acid sequence of insulin with chromatography and
fragments of polypeptide.
• Secondary Structure:
○ The coils and folds of polypeptide chains that contribute to the protein’s
conformation/
○ Polypeptide Backbone:
 H Bonds, partial negative charge. H bonds with N determine shape.
 Alpha Helix:
• Coils
• H bond ever 4th amino acid.
 Beta pleated sheet:
• Two or more regions of polypeptide chain
• Parallel to each other
• H bonds between parallel regions hold them together.
• Ex. Spider silk
 One protein can have both shapes in polypeptides.
• Tertiary Structure:
○ Irregular contortions from interactions between side chains of various amino
acids.
○ Hydrophobic Interaction:
 Non polar amino acid side chains cluster together with Van der Waals
forces, excluding water which H bonds to itself. This gives protein its
shape.
○ Disulfide Bridges:
 Covalent bonds that link two cysteine monomers (amino acids with
sulfhydryl group [--SH]) when they meet as protein folds.
 Two sulfides bond, folding the protein (-S-S-)
• Quaternary Structure:
○ Overall protein structure that results from the aggregation of polypeptide units.
○ Ex. Collagen: helical proteins make triple helix.
○ Ex. Hemoglobin: A lobular protein.
• Protein Conformation:
○ Determined by amino acids, secondary, and tertiary structures.
○ Also depends on environment.
• Denaturation:
○ Protein loses conformity because of environment.
○ Ex. Salt, pH, etc
○ Biologically inactive usually because it leaves aqueous environment to organic
solvent; bond disruption.
○ Remove denaturation agent back to normal because shape is intrinsic in
proteins.
• Difficult to trace “folding” path of protein.
○ Final step doesn’t show steps.
• Chaperonins/chaperone proteins:
○ Help proteins fold by making sure nothing bad happens to new protein (no bad
influence).
○ IBM computer Blue Gene to illustrate protein with amino acids.
○ X-ray Crystallography: Deflected beams from protein atoms in crystal to make
model.

Nucleic Acids: