Download MOLECULES OF LIFE

MOLECULES OF LIFE
CH 4 AND 5
Carbon is the building block of the molecules of life
Chemistry of Carbon
I.
A.
B.
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Functional Groups
Group of atoms linked to carbon that have specific properties
Hydroxyl ( OH)
o Forms hydrogen bonds
Carboxyl (COOH)
o Forms ionic bonds
Amino (NH2)
o Forms ionic bonds
Sulfhydryl (SH)
o Forms covalent bonds
Phosphate (PO4)
o Forms covalent bonds
o
C.
Macromolecules
 Large molecules many of which are polymers
 Polymer: a macromolecules made of repeating units called monomers
 Macromolecules are made by dehydration reactions: linking of
monomers together with the removal of water
 Macromolecules are broken down by hydrolysis reactions: breakdown
of a macromolecule with the addition of water
 The 4 macromolecules that make up all living things are:
o Proteins
o Carbohydrates
o Lipids
o Nucleic acids
II.
Carbohydrates
A.
Monosaccharides
1.
structure
2.
isomers
3.
function
B.
Disaccharides
1.
Structure
2. Function
C.
Polysaccharides
2 groups of polysaccharides
Storage: starch and glycogen
Structural: cellulose chitin
1. Storage polysaccharides
a. function
store glucose for later use
b. structure
 Glycogen
 Starch
2.
structural polysaccharides
a.
cellulose
b.
chitin
III.
Lipids
Diverse group of hydrophobic molecules
B.
Triglycerides (fats and oils)
1.
structure
2.
Fatty Acid
 Long chain of C and H with a carboxyl group
 Usually 14 to 20 Cs
 Fatty acids can be
o Saturated:
o Monounsaturated:
o Polyunsaturated:
3.
C.
D.
E.
Function
Phospholipids
1.
Structure
2.
Property
Amphiphathic:
3.
Function:
Waxes
Function as protective barrier
Steroids
Function as chemical messengers
IV.
Proteins
Large polymer made of repeating monomers called amino acids
A.
Functions of Proteins
 Enzymes: catalyze cell’s reactions
 Defense: antibodies destroy foreign invaders
 Transport: move molecules around body and into and out of
cells
 Support and structure: long fibrous proteins in hair nails skin
 Movement: contractile proteins in cells
 Regulation: proteins involved in maintaining homeostasis
B.
Amino Acids
1.
general structure
2.
Groups of amino acids: based on the characteristics of R
group
Nonpolar
Glycine
(Gly or G)
Alanine
(Ala or A)
Leucine
(Leu or L)
Valine
(Val or V)
Isoleucine
(Ile or I)
Proline
(Pro or P)
Methionine
(Met or M)
Phenylalanine
(Phe or F)
Trypotphan
(Trp or W)
Polar
Serine
(Ser or S)
Threonine
(Thr or T)
Cysteine
(Cys or C)
Tyrosine
(Tyr or Y)
Asparagine
(Asn or N)
Glutamine
(Gln or Q)
Electrically
charged
Acidic
Aspartic acid
(Asp or D)
Basic
Glutamic acid
(Glu or E)
Lysine
(Lys or K)
Arginine
(Arg or R)
Histidine
(His or H)
3.
C.
Linking of amino acids
 Linked together by dehydration reactions
Protein Structure
1.
General rules on protein folding
2.
There are 4 levels of protein structure
a. primary structure
b. secondary structure
c. Tertiary structure
d. Quaternary structure
Special proteins called chaperonins help proteins fold into their secondary
and tertiary structures
All proteins have primary and secondary structure
Most proteins have tertiary structure
Some proteins have quaternary structure
3.
Protein unfolding
V.
Nucleic Acids
The information molecules
Contain and express all of the hereditary info
A.
Structure
 Long chains of nucleotides linked via dehydration reactions
B.
Nucleotides
Made of a:
5 carbon sugar
Phosphate group
One of 4 bases
C.
Function
 DNA:
 RNA: