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Macromolecules
molecule composed of polymers.
-each MM has monomer, bonds that link them together, & their functions.
polymers
large molecules composed of multiple monomers
categories of macromolecules are defined by
monomers
Synthesis vs. Degradation
synthesis: builds macromolecules
degradation: breaks macromolecules down
condensation reactions
link monomers together (covalent bonds) to form a polymer (MM)
- water is a product of this reaction
hydrolysis reactions (water lysis)
water is used as a reactant to break macromolecules back into their individual monomers.
carbohydrates
MM with chemical formula (CH2O)n
-H & O ratio similar to water
-monomers are simple sugars
monosaccharides
simple sugars: glucose, fructose, galactose
polysaccharides
polymers of monosaccharides: cellulose, starch, glycogen
cellulose
a polymer of beta glucose monomers held together by beta linkages.
importance of cellulose
-provides shape & rigidity to plant cells
-important to humans (wood, heat, tools, etc.)
-not digestible
beta form of glucose formation
cellulose cable; 1 strand of cellulose; monomer of cellulose
Water = polar molecule
-Water held together by 2 covalent bonds
-Oxygen is much more electronegative than hydrogen (polar covalent bonds)
-Causes partial charges (water is polar)
hydrogen bonds
-attraction between a partially +H (polar covalent bond) & another atom with partially - atom
-need hydrogen donor & acceptor (partially - atom)
-1 H2O molecule can form 4 hydrogen bonds
Methane molecules
can't from hydrogen bonds; is a gas at room temp
hydrophilic
"water loving"
-polar molecules are soluble in water
hydrophobic
"water fearing" & antipathic
-nonpolar molecules are insoluble in water
Acid
donates protons (H+)
Base
accepts protons (H+)
High pH
OH- (base)
Low pH
H+ (acid_)
Independent variable (Lab 2)
pH
Dependent variable (Lab 2)
electrical charge of proteins
Proteins used in Lab 2
-Serum Albumen (blue)
-Cytochrome C (orange)
-Myoglobin (brown)
amino acids
monomers that build a protein
Alpha carbon
the central carbon atom of each amino acid (4 bones)
Amino acid structure

R group
this is what differs amino acids.
-ionic, polar, or non-polar
-ionic matters for electrophoresis
pH
the negative logarithm of the hydrogen ion concentration
- (mol/L) (-log[H+])
-1 unit change in pH = 10 fold change in H+ concentration
pH scale
0 (acidic) to 7 (neutral) to 14 (basic)
Neutral pH
[H+] = [OH-]
- Isoelectric point: where an individual molecule has no net charge (could theoretically be any pH)
Acidic pH
[H+] > [OH-]
Basic pH
[H+] < [OH-]
Proteins
polymers of amino acids linked by peptide bonds
amino acids with ionic R groups
aspartic acid, glutamic acid, lysine, arginine, and histidine
How do proteins become charged?
- Amino groups gain at low pH (H+ , attracted to - pole)
- Carboxyl group lose at high pH (OH- , attracted to + pole)