3,4 b130carbon,polymers
TRANSCRIPT
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Carbon and organic molecules
Carbon and its bonds
Polymers and monomers
- Carbohydrates
- Proteins
- Lipids- Nucleic acids
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A carbon atom forms four covalent bonds
C can make chains or rings
Why is carbon so important to molecules of life?
Figure 3.1, top part
Structuralformula
Ball-and-stickmodel
Space-fillingmodel
Methane
The 4 single bonds of carbon point to the corners of a tetrahedron.
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Methane, CH4
Figure 2.8Bx
Arrangement of atoms determines molecular shape.
Shape determin
es function of molecules
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Butane, ball and stick model
Figure 3.1x3
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What affects solubility in water?
Molecules with +/- charge are usuallyhydrophilicor water-loving
Molecules with no charge and non-polar areusuallyhydrophobic and not soluble in water
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Polymers are long chains of smaller molecularunits called monomers
A huge number of different polymers can be
made from a small number of monomers
How do cells make so many different moleculesthat are needed for life?
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are single-unit sugars
a multiple of CH2O
fuels forcellular work
Monosaccharides
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Carbohydrates
DISACCHARIDES ANIMATION
Figure 2.12a
b
PRESSTO PLAY
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Molecules, including non-sugars, taste sweet
because they bind to sweet receptors on thetongue
Why is sugar sweet?
Table 3.6
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disaccharides
Glucose Glucose
Maltose
Figure 3.5
Sucrose
glucose fructose
Dehydration synthesis
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Polysaccharides are long chains of sugar units
Size: thousands of linked monosaccharides
purpose: energy storage, structural
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Starch (plants) and glycogen (animals)
Cellulose (plants) and chitin (insects, fungi)
Figure 3.7
Starch granules inpotato tuber cells
Glucosemonomer
STARCH
GLYCOGEN
CELLULOSE
Glycogen granulesin muscle tissue
Cellulose fibrils ina plant cell wall
Cellulosemolecules
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Starch Cellulose
Figure 3.7x
= fiber
Indigestible by animals
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hydrophobic
composed largely of carbon and hydrogen
Purposes:
- energy storage
- insulation, cushioning
- membranes
- signals
Lipids include fats, oils, and steroids.
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Fats are triglycerides
one glycerol molecule linked to three fatty acids
fatty acid chains often differ
Fatty acid
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Saturated fats lack double bonds
solid at room temperature (lard)
Fatty acids of unsaturated fats contain doublebonds
liquid at room temperature (plant oils)
Trans fats have wrong way double bonds
Figure 3.8C
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Waxes form waterproof coatings and can preventorganisms from drying out or getting wet
QuickTim e and a TIFF (Uncompressed) decompressor are needed to see this picture.
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Steroids are often hormones
testosteroneestrogen
Anabolic steroids
Hormone Replacement
Therapy
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Cholesterol
Membranes
Precursor toVitamin D,
bile salts
Figure 3.9x1
HDL High Density Lipoprotein
LDL Low Density Lipoprotein
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Proteins are involved in
cellular structure
movement
nutrition
defense
transport
communication
Enzymes regulate chemical reactions
Proteins are essential to the structures andactivities of life
Figure 3.11
P t i th t t t ll d
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Their diversity is based on differentarrangements of amino acids
Proteins are made from just 20 kindsof amino acids
Proteins are the most structurally andfunctionally diverse of lifes molecules
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Each amino acid contains:
an amino group
a carboxyl group
an R group, which distinguishes each of the 20
different amino acids
Aminogroup
Carboxyl (acid)groupFigure 3.12A
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Each amino acid has specific properties
Leucine (Leu)
Figure 3.12B
Serine (Ser) Cysteine (Cys)
HYDROPHOBIC HYDROPHILIC
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Cells link amino acids together by dehydration
synthesis
Peptide bonds
Amino acid Amino acid Dipeptide
Dehydration
synthesis
Carboxylgroup
Aminogroup
PEPTIDEBOND
Figure 3.13
A t i ifi h d t i it f ti
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A protein consists of polypeptide chains foldedinto a unique shape
shape determines the proteins function
A protein loses its function when itspolypeptides unravel
A proteins specific shape determines its function
Figure 3.14A Figure 3.14B
A t i i t t i it i id
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A proteins primary structure is its amino acidsequence
Secondary structure is polypeptide coiling or
folding produced by hydrogen bonding
Figure 3.15, 16
Amino acid
Hydrogenbond
Alpha helix
Pleated sheet
Primary
structure
Secondarystructure
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Tertiary structure is the overall shape of apolypeptide
Quaternary structure is the relationship among
multiple polypeptides of a protein
Figure 3.17, 18
Polypeptide(single subunitof transthyretin)
Transthyretin, with fouridentical polypeptide subunits
Tertiarystructure
Quaternarystructure
E bl
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Enzyme(sucrase)
Activesite
1
2
3
Substrate(sucrose)
Enzyme availablewith empty activesite
Substrate
binds toenzyme withinduced fit
Substrate isconverted to
products
4
Products arereleased
Glucose Fructose
enzyme isunchanged andcan repeat theprocess
Figure 5.6
A specific
enzyme
catalyzes
each cellular
reaction
Enzymes enable
chemical reactions
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What can denature a protein?
High temperature
pH, low or high
High salt concentration
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Nucleic acids such as DNA and RNA serve asthe blueprints for proteins
They ultimately control the life of a cell DNA sequence is inherited by progeny
Nucleic acids are information-rich polymers ofnucleotides
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The monomers of nucleic acids are nucleotides
Phosphategroup
SugarFigure 3.20A
Each nucleotide is composed of a sugar,phosphate, and nitrogenous base
Nitrogenousbase (A)
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The sugar and phosphate form the backbonefor the nucleic acid
Sugar-phosphatebackbone
Nucleotide
Figure 3.20B
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DNA consists of twopolynucleotides held
together by hydrogen bonds
Figure 3.20C
The sequence of the
four kinds ofnitrogenous bases inDNA carries geneticinformation
Nitrogenousbase (A)
Basepair
Adenosine triphosphate (ATP)
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Copyright 2003 Pearson Education, Inc. publishing as Benjamin Cummings
Adenosine triphosphate (ATP)
Chemical energy used by allcells
Energy is released by breakinghigh energy phosphate bond
ATP is replenished byoxidation of food fuels
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How ATP Drives Cellular Work
Figure 2 20
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