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excess glucose
⎯ “giant” molecules that are formed by
molecules
the joining of many smaller • Protein
ii. glycogen- how
molecules ⎯ C, H, O, N sometimes S
animals store
Polymer ⎯ amino acid: monomer
excess glucose;
- 20 types
liver ⎯ long molecule consisting of many
a. amino group (-NH2)
2. structural similar or identical building blocks
b. carboxyl group (-COOH)
i. cellulose – forms linked together by covalent bonds
c. carbon
the tough, fibrous
d. r group
material found in
⎯ function: to the formation of Peptide Bond- covalent bond
a. Enzymes hydrogen bonds at formed by a dehydration reaction
b. Hormones regular intervals that links the carboxyl group of one
c. Transport (hemoglobin) 3. Tertiary amino acid to the amino group of
d. Contractile (muscle tissue) - irregular contortions of another amino acid
e. Antibodies a protein due to
Polypeptide- chain of amino acids
f. Membrane structure bonding between side
held together by peptide bonds; not
g. Structural proteins chains; gives the
yet a fully functioning protein
⎯ “As proteins go, shape protein its shape; due
determines function.” to hydrophobic
⎯ Denatured protein interactions and • Lipids
- has lost its unique, 3-D disulfide bridges ⎯ C, H, O
shape; inactive and can no Hydrophobic Interaction- clustering ⎯ monomers:
longer carry out its of hydrophobic side chains at the 1. glycerol- 3 carbon
function center of the protein compound with hydroxyl
⎯ Levels of Organization on each carbon; no 1:2:1
Disulfide Bridges- Covalent bonds
1. Primary ratio
between the side chains of two
- unique sequence of 2. fatty acid- very long carbon
cysteine amino acids. The sulfur of
amino acids that are skeleton with a carboxyl
one cysteine bonds to the sulfur of the
put together by the group at one end
second.
ribosomes of the cell ⎯ use:
2. Secondary 4. Quaternary 1. good source of energy
- the initial folding and - two or more 2. used to insulate the body
shaping of the polypeptide subunits 3. cushion the internal organs
polypeptide. It is the combine to form a
repetitive folding due functional protein
4. phospholipids are a in the tail wherever a 2. hydrophobic fatty
structural component of double formed is acid tail- point to
membranes found each other across
⎯ characteristics: - “kinky tails” prevent the middle of the
• nonpolar them from packing membrane; make
• insoluble too close together; the membrane
a. Fat temperature
- vegetable oils • Nucleic Acid
i. Saturated Fatty Acid
b. Oil ⎯ C, H, O, N, P
- no carbon to carbon
c. Wax ⎯ types:
double bond; as
- used as a water 1. DNA
many hydrogen
proofing material on 2. RNA
atoms as possible are
leaves, fruits, ⎯ nucleotide
bonded to the carbon
atoms feathers, fur 1. sugar