Outer shell of carbon has 4 electrons (AKA tetravalent); can
hold 8 Each carbon atom can form covalent bonds with up to four
other atoms This electron structure allows carbon to bond with
itself easily as well as other atoms (creates a wide variety &
abundance or organic compounds)
Slide 4
structural formula for methane ball-and-stick model
space-filling model p.34b
Slide 5
Carbon atoms can form chains or rings Other atoms project from
the carbon backbone
Slide 6
or p.34e Simplified structural formula for a six-carbon ring
icon for a six-carbon ring Organic Compounds
Slide 7
Ex: butane C 4 H 10
Slide 8
Atoms or clusters of atoms that are covalently bonded to carbon
backbone Give organic compounds their different properties All are
hydrophilic except for one
Slide 9
Hydroxyl group - OH Amino group- NH 3 + Carboxyl group- COOH
Phosphate group- PO 3 - Sulfhydryl group- SH Carbonyl -COH
Methyl-CH 3
Slide 10
Fig. 3-4, p.36
Slide 11
Estrogen and testosterone are hormones responsible for
observable differences in traits between male and female wood ducks
Differences in position of functional groups attached to ring
structure (pg 36) An EstrogenTestosterone
Slide 12
Large molecules made of many similar smaller building blocks
called MONOMERS Are formed and broken by adding or removing
water
Slide 13
The loss of water Monomers bond together to make polymers
Requires energy (endothermic)
Slide 14
Condensation Fig. 3-6a, p.38
Slide 15
Adds water Breaks polymers into monomers Gives off energy
(exothermic) Ex: digestion
Slide 16
Hydrolysis Fig. 3-6b, p.38
Slide 17
Carbohydrates Lipids Proteins Nucleic Acids
Slide 18
The bodys main source of energy Monomer is a monosaccharide
Contain carbonyl functional group
Slide 19
Simplest General formula is C n H 2n O n Most have 5- or
6-carbon backbone Glucose (6 C)Fructose (6 C) Ribose (5
C)Deoxyribose (5 C)
Slide 20
glucosefructose Fig. 3-7, p.38
Slide 21
Type of oligosaccharide Two monosaccharides covalently bonded
by a Glycosidic Bond Formed by condensation reaction Ex: sucrose
and maltose (isomers) + H 2 O glucosefructose sucrose Fig. 3-7b,
p.38
Slide 22
Straight or branched chains of many sugar monomers linked by
condensation Most are for structural or storage purposes Ex:
Cellulosein plant cell wall Starch (such as amylose)sugar storage
in plants Glycogensugar storage in animal muscle & liver cells
(when blood sugar drops, glycogen is broken down to glucose)
Chitinin arthropod exoskeleton & fungal cell wall
Slide 23
Fig. 3-8, p.38
Slide 24
Fig. 3-9, p.38
Slide 25
Polysaccharide Nitrogen-containing groups attached to glucose
monomers Structural material for hard parts of invertebrates, cell
walls of many fungi
Slide 26
http://www.youtube.com/watch?v=_zm_DyD6F J0
Slide 27
Fats Phospholipids Waxes steroids Tend to be insoluble in water
(hydrophobic)
Slide 28
Monomer is 3 Fatty acid(s) attached to glycerol Triglycerides
are most common Linked by ester bonds Fig. 3-12, p.40
Slide 29
Carboxyl group (-COOH) at one end Carbon backbone (up to 36 C
atoms) Saturated - Single bonds between carbons with max. amt. of H
Unsaturated - One or more double C bonds
Slide 30
Three Fatty Acids Fig. 3-11, p.40
Slide 31
Main components of cell membrane Monomer is 1 glycerol + Fatty
acids
Slide 32
No fatty acids four fused-together carbon rings with
hydrocarbon tail Ex:Cholesterol & hormones such as cortisol,
testosterone, estrogen, and adrenaline Fig. 3-14, p.41
Slide 33
http://www.youtube.com/watch?v=VGHD9e3y RIU
Slide 34
Monomer is amino acids linked by peptide bonds (formed by
condensation)
Slide 35
Enzymesspeed up rxns (Ex: catalase & pepsin) Contractilefor
movement (Ex: myosin in muscle cells) Structuralin hair & nails
(Ex:collagen, elastin, keratin) Storage Ex: casein Transport Ex:
hemoglobin (contains heme group) HormonesEx: insulin
Linear Sequence of amino acids Two linked amino acids =
dipeptide Three or more = polypeptide Backbone of polypeptide has N
atoms: -N-C-C-N-C-C-N-C-C-N- one peptide group
Slide 40
a Normal amino acid sequence at the start of a beta change for
hemoglobin VALINE HISTIDINELEUCINETHREONINEPROLINEGLUTAMATE Fig.
3-18a, p.45
Slide 41
VALINE HISTIDINELEUCINETHREONINEPROLINEVALINEGLUTAMATE b One
amino acid substitution results in the abnormal beta chain in HbS
molecules. During protein synthesis, valine was added instead of
glutamate at the sixth position of the growing polypeptide chain.
Fig. 3-18b, p.45
Slide 42
c Glutamate has an overall negative charge; valine has no net
charge. The difference gives rise to a water-repellant, sticky
patch on HbS molcules. They stick together because of that patch,
forming rod- shaped clumps that distort normally rounded red blood
cells into sickle shapes. (A sickle is a farm tool that has a
crescent-shaped blade.) sickle cell normal cell Fig. 3-18c,
p.45
Slide 43
Hydrogen bonds form between different parts of polypeptide
chain These bonds give rise to coiled or extended pattern Alpha
Helix or beta pleated sheet
Slide 44
Slide 45
Folding as a result of interactions between R groups Involves
disulfide bonds heme group coiled and twisted polypeptide chain of
one globin molecule
Slide 46
final protein structure formed by interaction of 2 or more
polypeptide chains Hemoglobin
Slide 47
heme alpha globin beta globin Fig. 3-17, p.44
Slide 48
Lipoproteins Proteins combined with cholesterol, triglycerides,
phospholipids Glycoproteins Proteins combined with
oligosaccharides
Slide 49
Disruption of three-dimensional shape (unraveling of its shape)
Causes of denaturation: pH Temperaturecooking an egg denatures the
egg whites albumin which goes from clear to white salinity
Destroying protein shape disrupts function
Slide 50
Chaperone proteinsassist proteins with their folding
Vitaminsmay acts as coenzymes
Slide 51
http://www.youtube.com/watch?v=2Jgb_DpaQ hM
Slide 52
Composed of monomers called nucleotides Adenine Cytosine
5 C Sugar Ribose or deoxyribose phosphate group Nitrogen Base
(A, C, G, T, U) Single or double ring structure
Slide 55
Slide 56
Slide 57
three phosphate groups sugar base
Slide 58
THYMINE (T) base with a single-ring structure CYTOSINE (C) base
with a single-ring structure Fig. 3-20, p.46
Slide 59
A, G Larger (double rings) C, T, U Smaller (single rings)
Slide 60
Double-stranded Consists of four types of nucleotides A bound
to T C bound to G
Slide 61
Usually single strands Four types of nucleotides Unlike DNA,
contains the base uracil in place of thymine Three types are key
players in protein synthesis
Slide 62
Slide 63
Make sure you color the label the same color as the actual
structure. Ex: enzyme (A)if you choose to color the label red, the
structure A must also be red