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Bio Notes  Energy Source

Glycolysis, Kreb’s Cycle, Cellular


Macromolecules – large molecules
Respiration
 CHO,PRO, Nucleic acid  Metabolic Primer – starter of metabolic
processes
Macromolecules are polymers built from  Protein Spare
monomers  Central Nervous System Fuel – 70% of
intake sugar goes to the brain
 Polymer – long molecule consisting of
identical building blocks linked by
 Polysaccharide – carbohydrate
covalent bonds
macromolecule polymer composed of
 Monomers – repeating units that serve as
many sugar blocks
building blocks
Sugars
Synthesis and Breakdown of Polymers
(sugar template = carboxyl group +
 Enzymes – specialized macromolecules
multiple hydroxyl group)
that speed up reactions
 Monosaccharide – simple sugar
 Dehydration reaction – forms new bond ;
-multiple of CH2O
loss of water molecule
 Glucose – most common monosaccharide
-also called as Polymerization
 Aldose(aldehyde sugar) – carbonyl group
 Hydrolysis – breaks a bond; addition of
at the end of carbon skeleton
water molecule
-ex. Glucose, Galactose
-ex. digestion
 Ketose(ketone sugar) – carbonyl group
DR.  HR.
within carbon skeleton
(short polymer + unlinked monomerOH
-ex. Fructose
 longer polymer + H2O)

Diversity of Polymers Triose – 3carbon sugar(Glyceraldehyde,


Dihydroxyacetone)
Polymers are constructed from only 40-50 Pentose – 5carbon sugar(Ribose,
common monomers Ribulose)
Hexose – 6carbon sugar(glu, galac, fruc)
Four Major Classes of Large Biological
Molecules: Carbohydrates, Protein, Lipids,
 Disaccharide – consists of 2
Nucleic Acid
monosaccharides joined by glycosidic
*Note that on the molecular scale lipids is linkage; simple carbohydrates
not a macromolecule because of its size Glu + Glu = Mal
Glu + Galac = Lac
Carbohydrates (C6H12O6) Glu + Fru = Suc
-sugar, starch, fiber  Glycosidic linkage – covalent bond
formed by dehydration rxn
Functions
 Lactose Intolerance – condition in Viscous vs Non Viscous
humans who lack lactase, the enzyme Fermentable vs Non Fermentable
that breaks down lactose. Sugar is instead  Chitin – carbohydrates used by
broken down by the intestinal bacteria, arthropods(insect, spider, crustacean,
causing formation of gas and often etc.)
cramps -exoskeleton of arthropods, cell wall
 Polysaccharide – polymers with a few material of fungi
hundred to thousand monosaccharide -beta linkage
joined by glycosidic linkage  Insulin – too much sugar(hyperglacemia),
 Starch – carbs bank/storage for plants triggers lowering of blood sugar;
-polymer of glucose monomers, as formation of glycogen
granules within cellular structures known  Glucagon – too low sugar(hypoglacemia),
as plastids triggers increase of blood sugar; breaking
-ex. Potato tubers, grains: fruits of wheat, down of glycogen to glucose
corn, rice  Type 1 Dia – IDD, Type 2 Dia – NIDD,
 Amylose – simplest form of starch, not Predia – HBS not in range
branched/linear
 Amylopectin – more complex starch,
Lipids
branched polymer w/ 1-6 linkages at
branch points -mix poorly with water
 Glycogen – carbs bank/storage for
animals -not big enough to consider as a
-polymer of glucose that is like macromolecule
amylopectin but more extensively
-fats, phospholipid, steroids
branched
 Cellulose – polysaccharide, major Functions
component of the tough walls that
enclose plant cells  Energy Storage
-most abundant organic compound in  Insulation
Earth  Protection
-abrades the digestive tract and  Shock Absorption
stimulates the lining to secrete mucus,
which aids in the smooth passage of food  Fats – not polymers; constructed from
in the tract two kind of molecules: glycerol and fatty
acids
Starch vs Cellulose  Glycerol – an alcohol; each of its 3 carbon
Alpha linkage vs beta linkage bears OH
Same orientation vs upside down w/  Fatty Acid – long carbon skeleton; at one
repect to neighbour end has CO
 Fiber –ruminants  Ester linkage – bond formed by
Soluble vs Insoluble dehydration reaction in fats
 Triacylglycerol/Triglyceride – consists of 3  Storage protein – storage of amino acids;
fatty acids linked to one glycerol molecule ex. Casein, the protein of milk, is major
 Saturated Fat – no double bonds in source of amino acids for baby mammals.
carbon, no bending, solid in room temp Plants have storage in seed. Ovalbumin is
 Unsaturated Fat – one or more double the protein of egg whites
bonds of carbon, cis bonds cause  Transport protein – transport of
kinks/bendings substances; Hemoglobin, the iron-
 Hydrogenated fats – trans fat, addition of containing protein of vertebrate blood,
H2O allowing them to solidify transports oxygen from lungs to other
 Phospholipids – major constituents of cell part of the body.
membranes; similar to fat molecules but  Hormonal protein – coordination of an
have only two fatty acids attached to organism’s activities; ex. Insulin, a
glycerol cuz the third hydroxyl group of hormone secreted by the pancreas,
glycerol is attached to phosphate group causes other tissues to take up glucose,
thus regulating concentration
Hydrophilic head – loves water  Contractile and motor protein –
Hydrophobic tail – fears water movement; Motor proteins are
Bilayer – when phospholipids are added responsible for the undulations of cilia nd
to water, they assemble to this double- flagella. Actin and myosin are responsible
layered sheet for the contraction of muscles
 Steroids – lipids characterized by a  Receptor proteins – response of cell to
carbon skeleton consisting of four fused chemical stimuli; ex. Receptors built into
rings the membrane of a nerve cell detect
 Cholesterol – type of steroid signalling molecules released by other
nerve cells
 Structural proteins – support; ex. Keratin
Protein is the protein of the hair, nails, horns,
-proteios = first/primary feathers, etc. Insects and spiders use silk
fibers to make cocoons and webs.
-constructed from the same set of 20 Collagen provide fibrous network in
amino acids, linked in unbranched polymers animal connective tissues

Functions
 Peptide Bond – bond between amino
 Enzymatic protein – selective acceleration acids
of chemical reactions; ex. Digestive  Polypeptide – polymer of amino acids
enzymes catalyse the hydrolysis of bonds  Protein – biologically functional molecule
of foods made up of one or more polypeptide
 Defensive protein – protection against
Amino Acid Monomers
disease; ex. Antibodies inactivate and
help destroy viruses and bacteria  Amino Acid – organic molecule with both
amino group and carboxyl group
Protein Structure
Side chain(R group)
| Primary – linear chain of amino acids
(NH2) (C) (CHO2) Secondary – regions stabilized by
Amino -- Alpha -- Carboxyl hydrogen bonds between atom of the
Group Carbon Group polypeptide backbone
(N-terminus) (C-terminus)
(Polypeptide Backbone) Alpha helix – coiled
|
Beta pleated sheet – folded
H
Tertiary – Three-dimensional shape
20 Amino Acids of Proteins stabilized by interactions between side
Nonpolar side chains; hydrophobic chains
-Glycine/Gly/G
-Alanine/Ala/A Disulfide bridges – covalent bonds that
-Valine/Val/V reinforce the shape of protein
-Leucine/Leu/L
Quaternary – Association of two or more
-Isoleucine/Ile/I
polypeptides(some proteins only)
-Methionine/Met/M
-Phenylalanine/Phe/F single amino acid substitution causes Sickle-
-Tryptophan/Trp/W cell disease.(glu becomes val in the sixth
-Proline/Pro/P position of amino acids in hemogoblin)
Polar side chains; hydrophilic
-Serine/Ser/S Key Factors that determine protein structure
-Threonine/Thr/T
-pH, temperature, salt concentration,
-Cysteine/Cys/C
specific part=specific function and factor
-Tyrosine/Tyr/Y
-Asparagine/Asn/N
-Glutamine/Gln/Q  Enzyme – type of catalytic protein
Electrically charged side chains;  Activation Energy – energy barrier/energy
hydrophilic needed to convert rct to prod
(acidic - )
-Aspartic acid/Asp/D Oxydoreductase – redox rxn
-Glutamic acid/ Glu/E
transterases –
(basic + )
-Lysine/Lys/K hydrolase – hydrolysis rxn
-Arginine/Arg/R
-Histidine/His/H lyase – dehydration

isomenases –
 Globular proteins – spherical in structure
 Fibrous proteins – shaped like long fibers ligases – ex. Dna ligase
 Denaturation of protein – deterioration
of enzyme
 Cofactors – helpers of enzymes

 Sd
 Sd

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