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What Is Life?
Cell
-Basic unit of life - Smallest unit with the capacity to live and reproduce, independently or as part of a multicellular organism
When were cells first observed? a.Early 1400s b.Late 1500s c. Mid 1600s d.Early 1800s e.Early 1900s
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Origin of the term 'cell. Robert Hooke is credited as the originator of the term cell, which he used in his description of the structure of cork. This illustration is taken from his book on microscopy, referred to as 'Micrographia'.
A Very Brief History of Cytology (Cell Biology) 1838 Cell Theory put forth by Schleiden & Schwann German scientists and colleagues Schleiden was was a botanist
Observed cell division in plants
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All provided important contribution that helped create a foundation for Cell Biology
Human Cells:
FYI: Estimated that the average human body has ~30+ trillion cells!
Source: Bianconi et al. (2013) Annals of Human Biology.40, 463-471
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There are ____different Domains of living organisms recognized in the contemporary phylogenetic tree of life.
a) b) c) d) e) two three four five ten
Tree of Life
Tree of Life is continually being redrawn
Earlier classification systems based largely on morphological characteristics Scala naturae (350 BC)
Classification scheme outlined in Aristotles History of Animals All matter organized as decreed by God Definition of terms still used today: Vertebrates/Invertebrates
2 kingdoms (1700s)
Classification pioneered by Carl Linneaus & his bionomial taxonomy Everything was either a Plant or an Animal Bacteria were considered plants
5 kingdoms (1960s)
Monera (prokaryotes), Protista, Plantae, Fungi, Animalia FYI: Original paper published in Science:
Whittaker R.H. (1969). Science 163:150160.
http://www.sciencemag.org/content/163/3863/150.full.pdf?ijkey=e364e760bafd3ddb27f995f0c1e9b08fdf28eb0f&keytype2=tf_ipsecsha
Tree of Life
Current Phylogeny = 3 Domain system
Bacteria = Prokaryotes Archaea = Prokaryotes, many extremophiles Eukarya = Eukaryotes
Group includes Protists, Plants, Fungi, Animals
3 Domains of Life
Hypothetical Phylogenetic Tree of Life
~3.5 BYA
*Note: Origins of LUCA and Eukarya lineage are hypothetical Reviews - Nature 440: 623-630; BioEssays 29: 74-84
3 Domains of Life
rRNA analysis revealed two separate groups of prokaryotes:
- Bacteria - Archaea
Also suggests that eukaryotes and archaea are more closely related to each other than to bacteria
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Protists
Many diverse lineages of various eukaryotic organisms
Can be unicellular
e.g. dinoflagellates
Red tide dinoflagellate
Can be multicellular
e.g. some algae species
kelp
Figure 4-3
Micrometer (m) is the most useful unit for expressing the size of cells and larger organelles
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Fig 1A-1
Nanometer (nm) -orAngstrom () are the units used to express size of molecules and smaller subcellular structures
= 70
= 70-80
= 20
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Fig 1A-2
* * *
Base Unit
* * * * * * *
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2 nm x 1 /0.1 nm = 20
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Units Worksheet
- Posted on Blackboard (along with KEY) under Course Documents - This is for your own practice. - This will not be handed in for assessment, but you are responsible for this material
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- Smallest unit with the capacity to live and reproduce, independently or as part of a multicellular organism
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Cell Size
growth
mitosis
3 Time
Q: Why dont the yeast cells just keep growing and growing? Why arent we just one giant cell?
Cell Size
growth
mitosis
3 Time
3) Rate of molecule diffusion within cell 4) Maintenance of adequate local concentrations of molecules within cell
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Cell 1
Cell 2
Multicellular Organism 1
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Cell Size
growth
mitosis
3 Time
Cell 1
Cell 2
Multicellular Organism 1
Lower SA to V ratio
leads to
Cell Size
Time
Fig 19-32
Figure 4-2
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12
Figure 11-4
b) Cell 2: 5m x 5m x 5m
c) Organism 3: 125(1mxm1xm1) d) Cell 4: 0.125m x 5m x 200m
5
200
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0.125
Strategies to Increase Surface Area Long, thin cells greater surface area:volume
Muscle fiber
Neuron
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What about egg cells? Do egg cells break the SA:V rule?
Figure 1. Comparisonof egg sizes. Ostrich egg (right), compared to chicken egg (lower left) and quail eggs (upper left).
Photo by Rainer Zenz.
Metabolically inactive Mostly lipids (fats), storage materials Actual viable cell component is very small
May involve:
Cytoskeleton
- Motor proteins + filamentous tracks
Carrier Proteins
- Transport across membranes
http://bio1151.nicerweb.com/med/Vid/Campbell7e/CytoplasmicStream-V.swf
Question to ponder: What factors make it possible for eukaryotic cells to be so much larger than prokaryotic cells?
Ave. Size of Prokaryotic Cell ~1-5 um diameter Ave. Size of Eukaryotic Cell ~10 100 um diameter
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Eukaryotic Cell
e.g. typical Animal cell
ENDOPLASMIC RETICULUM (ER)
Smooth ER
Plasma membrane
CYTOSKELETON
Microfilaments Intermediatefilaments Microtubules
Ribosomes
Microvilli
Golgi apparatus Peroxisome Mitochondrion Lysosome Similar to Fig 4-5
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Eukaryotic Cell
e.g. typical Plant cell
Nuclear envelope NUCLEUS
Nucleolus Chromatin
Centrosome
Central vacuole
Golgi apparatus
Mitochondrion Peroxisome Plasma membrane Cell wall Plasmodesmata Wall of adjacentcell Chloroplast
In plant cells but notanimal cells: Chloroplasts Central vacuole and tonoplast Cell wall Plasmodesmata
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Cell Fractionation
Separation of a cell structures/components Two phases 1. Homogenization
lysing cells open chemicals, enzymes, or sound waves
2. Centrifugation
Homogenize tissue
Mouse liver
Centrifugation
Use of centrifugal force to separate mixture(s)
Fixed-angle Swinging-bucket
Similar to Figure12A-2
Larger/denser objects sediment more quickly (large S value) Smaller/ less dense objects sediment less quickly (smaller S value)
Figure 12A-3
Cytoplasm
- Internal contents of cell - Contains: Cytosol
~semi-fluid material Organelles (eukaryotes)
Subcellular structures
e.g. ribosomes
Plasma Membrane
4-8nm (40-80 ) thick layer of lipids + protein Boundary between cell and external environment
- defines cell - regulates movement in/out - mediates communication with external environment (e.g. receptors)
Fluid Mosaic
- many components (mosaic) - flexible, dynamic structure; not static
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Functions
mechanical strength growth/development protection
Fig 17-24
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Archaea
4 known variations: a. Sulfated polysaccharides b. Glycoproteins stabilized by Na+ c. S-layers protein chain mail d. Pseudomurein (shown below)
NAG NAT polysaccharide Cross-linked with peptides
Gram stain
Tool to ID bacteria based on cell wall characteristics
Cells stained with violet dye Rinse with alcohol Stain again with counter-stain (usually red dye)
Lipopolysaccharide Peptidoglycan layer Plasma membrane Protein Grampositive bacteria 20 m Gramnegative bacteria
Cell wall
(a)
Gram-positive: -Simple cell walls - cell walls have large amount of peptidoglycan - traps violet dye in the cytoplasm - alcohol rinse does not remove the violet dye, which masks the added red dye. - Cells appear violet after counter-stain is added
(b)
Gram-negative: -Complex cell walls with less peptidoglycan - Cell wall located in layer between -PM and an outer membrane - outer membrane also has lipopolysaccharides -violet dye is easily rinsed from the cytoplasm, - cells appears pink/red after counter-stain is added
Examples of Pathogenic Gram Yersinia pestis (Plague) Bordetella pertussis (Whooping cough) Chlamydia tachomatis (STD)
Gram Stain
Used as a quick diagnostic tool Examples:
Classification of new species
Based on CW characteristics Also preserves shape (e.g. spiral, rods)
Abstract We performed a prospective study in patients with tunneled catheters to assess the validity of Gram stain and superficial culture for anticipating catheter exit-site infection and hemodialysis catheterrelated bloodstream infection. The sensitivity and negative predictive value were high, and we succeeded in identifying a subpopulation at low risk of infection. Diagn Microbiol Infect Dis. 2013 Dec 17. pii: S0732-8893(13)00650-0. doi: 10.1016/j.diagmicrobio.2013.12.008. [Epub ahead of print] Copyright 2013 Elsevier Inc. All rights reserved.
- Penicillin
Interferes with peptide synthesis and peptidoglycan cross-linking
Penicillium fungus (DIC image)
Fosfomycin
Interferes with peptidoglycan biosynthesis
Brightfieldimage of Streptomyces fradiae
Nucleus
Stores DNA = CONTROL CENTER Large organelle
~5-6um diameter ~10% total cell volume
Nuclear Pores
Regulated openings through Nuclear Envelope
Openings controlled by Nuclear Pore Complex (NPC) NPC controls movement of substances in/out of Nucleus
Q: What sorts of molecules are moving in/out of nucleus?
Nuclear Lamina
Network of intermediate filaments (components of the cytoskeleton)
Nucleolus
Region within the Nucleus Clustered regions of ribosomal RNA genes surrounded by specific RNAs & proteins Site of ribosomal subunit synthesis Q: How do ribosomal subunits exit the nucleus? Q: What happens after they leave the nucleus?
Nucleus
(SEM)
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Ribosome
Found in all cell types (pro/eukaryote),and certain organelles
Not an organelle
25 30 nm
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The process by which genetic information coded in messenger RNA directs the formation of a polypeptide sequence is called____________.
a) b) c) d) e) Transcription Transformation Translation Transgression None of the above
Eukaryote
MasteringBiology Assignments #1 and #2 were due today at 12:30pm Assignments #3 and #4 are now available. due at 12:30pm on 2/3/14 i.e. ONE week from the availability date
Source: Jiang et al. (2008). Isolation of neuronal chromatic from brain tissue. BMC Neuroscience 9, 42.
Ribosome
Found in all cell types (pro/eukaryote),and certain organelles
Not an organelle
25 30 nm
Eukaryote
Ribosome
Translation
Overview of Translation in Ch 22
Overview of Translation
AA1
tRNA carrying first amino acid UAC Anticodon 5 AUG Start codon
Large
AA1
AUG
mRNA
During initiation, the components of the translational apparatus come together with an mRNA, and a tRNA carrying the first amino acid (AA1) binds to the start codon (AUG).
Figure 22-7
Overview of Translation
AA1
tRNA carrying first amino acid: INITIATOR tRNA UAC Anticodon 5 AUG Start codon
Large
AA1
AUG ELONGATION 2
During elongation, amino acids are brought to the mRNA by tRNAs and are added, one by one, to a growing polypeptide chain.
AA2 AA3 AA4 AA5
mRNA
During initiation, the components of the translational apparatus come together with an mRNA, and a tRNA carrying the first amino acid (AA1) binds to the start codon (AUG).
AA1
Figure 22-7
Overview of Translation
AA1
tRNA carrying first amino acid UAC Anticodon 5 AUG Start codon
Large
AA1
AUG ELONGATION 2
During elongation, amino acids are brought to the mRNA by tRNAs and are added, one by one, to a growing polypeptide chain.
AA2 AA3 AA4 AA5
mRNA
During initiation, the components of the translational apparatus come together with an mRNA, and a tRNA carrying the first amino acid (AA1) binds to the start codon (AUG).
AA1
Completed polypeptide
Release factor
TERMINATION
3 During termination, a stop codon in the mRNA is recognized by a protein release factor, and the translational apparatus comes apart, releasing a completed polypeptide.
Figure 22-7
Please note: If these topics seem totally foreign to you, please review transcription/translation (Ch. 21 & 22)
Examples: - Tetracyclin
irreversibly binds to 30S subunit; prevents tRNA from entering A site on 70S ribosome
Spectinomycin
interferes with mRNA interaction with the 30S ribosome
Endomembrane System
Nuclear envelope
ER
Endomembrane System
System of membranes and internal spaces
ER lumen
Cisternae Ribosomes Transportvesicle Smooth ER Rough ER
200 m
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Rough ER
Large, flattened sheets Ribosomes temporarily bound to cytosolic side
= rough appearance
Produces proteins, glycoproteins Products are distributed throughout cell by transport vesicles
Other endomembrane components Secreted products
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Smooth ER
Lack ribosome
smooth appearance
Functions:
Lipid synthesis
e.g. cholesterol, steroids
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Nuclear envelope
ER lumen
ER Adaptations
Like most subcellular structures, the ER is dynamic Cells can adjust relative amounts in response to changing conditions
- Manufacture of complex carbohydrates - Sorts and packages molecules for transport to final destinations
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Figure 12-1
mRNA
Signal peptide
Signalrecognition particle (SRP)
ER membrane Protein
CYTOSOL ER LUMEN
SRP receptor protein
Hydrolases are enzymes (biological catalysts) which catalyze the hydrolysis of macromolecules. What exactly does a hydrolase do?
a) Adds a water molecule to a bond, causing it to break b) Adds a water molecule in order to form a bond c) Removes a water water molecule from a bond, causing it to break d) Removes a water molecule in order to form a bond e) I have no idea!
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Rough ER
cis Golgi
trans Golgi
Plasma membrane
Lysosome
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Amoeba proteusstained with pH-dependent dye. The dye becomes dark red in the acidic environment of the food vacuoles.
Contractile vacuoles
osmoregulation
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Central Vacuoles
Found in plant cells Hold reserves of important organic compounds and water Maintain fluid balance/ turgor
Central vacuole
Cytosol Tonoplast
Central vacuole
5 m
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Food Vacuoles
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http://www.linkpublishing.com/video-transport.htm#Paramecium_-_Contractile_Vacuoles
Energy-converting Organelles
Mitochondrion Chloroplast
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Chloroplasts
Found only in photosynthetic eukaryotes Sites of photosynthesis
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Smaller cel taken inside another cell (larger prokaryote) Symbiotic relationship developed Dependency increased over time such that cells became ONE
What evidence might support the Endosymbiotic Theory for the Origin of Mitochondria & Chloroplasts?
Evidence Supporting the Endosymbiotic Theory for the Origin of Mitochondria & Chloroplasts
1) 2) 3) Mit/cp Similar size to prokaryotes (~1 um) Replicate by binary fission Double membrane
Inner membrane similar to prokaryotes, outer membrane may have been derived from host phagosome
4) 5) 6)
70S ribosomes
Sensitive to some antibiotics
Circular genome
Prokaryotic promoters, no histones
Peroxisomes
Similar in shape & size to lysosome
However, NOT part of endomembrane system
~Figure 4-19
Peroxisomes
Other functions: Breakdown of long-chain fatty acids
- via -oxidation pathway (more on this later)
Photorespiration in Plants
- Strategy to recover carbon that would be otherwise lost (more
on this later)
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Figure 4-20
1 m
Cytoskeleton
Network of protein fibers and associated proteins Network extends throughout the cytoplasm and underlie nuclear envelope Organizes structures and activities in the cell
Microtubule
0.25 m
Microfilaments
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Table 15-1
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Cell Locomotion
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signal
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signal
53
signal
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Proteobacteria
Homework:
Based on what we have discussed, describe, step by step, the pathway taken by hydrolase enzymes in order to localize them to the lumen of the lysosome. Start with transcription of the hydrolase gene.
Lysosome
Hydrolase ?
Figure 12-1
Figure 12-9
signal
11
signal
12
signal
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Tuberculosis
Infectious disease caused by mycobacteria strains WHO estimates 1/3 of the world population infected with mycobacteria Commonly affects lungs
Aerial transmission (e.g. coughing, sneezing)
CASE STUDY: Examination of white blood cells taken from a patient with tuberculosis reveals living bacteria in large vesicles. Continued observation over time shows that the bacteria remain alive for a long time.
In this case, which white blood cell process might be defective?
[EM image of] Mycobacterium tuberculosis phagosome in alveolar macrophage from an individual co-infected with HIV. Arrowhead, phagosome with M. tuberculosis. Arrows, virus-like particles suspected to be HIV buddinginside the macrophage.
Scale bar = 1 m. Annu. Rev. Cell Dev. Biol. 2004. 20:36794
Examination of white blood cells taken from a patient with tuberculosis reveals living bacteria in large vesicles. Continued observation over time shows that the bacteria remain alive for a long time. In this case, what white blood cell process might be responsible? a) Deficient receptors on the white blood cell for detecting bacteria b) Slow white blood cell motility c) Failure of the phagocytic vesicle and lysosome to fuse
~25 of all known elements are needed for life Of those, 5 are found in all living things
H, C, N, O, P
5 elements found in all living things Constitute 99% of an organisms weight Incomplete outer e- shells
donate, accept or share electrons to form ions and molecules i.e. they are REACTIVE
a) b) c) d) e)
Anatomy of an Atom
Atom = basic unit of matter
Nucleus surrounded by electrons
Electrons:
-ve charged particles
Electrons
Attracted to positively-charged nucleus
have potential energy because of attraction to the nucleus
Can have only certain amounts, or levels, of energy E levels are called electron shells
pictured as spherical regions around the nucleus
Valence Electrons
Electrons in the last shell Valence # = Group # (disregarding transition metals) Important determinant of reactivity
Can be gained or lost in a chemical reaction Atoms tend to react in ways that result in filled outer shell
Electronegativity
Affinity of an atom/molecule for electrons Electronegativity Scale:
The greater the EN value, the stronger the affinity for electrons
Types of Bonds
Ionic bond
Formed through electrostatic attraction between oppositely charged ions. Due to the attraction between:
an atom that has lost 1 or more electron (e.g. cation+) and an atom that has gained one or more electrons (e.g. anion-)
Ionic bond
Nonpolar +
Polar
Covalent bonds
Ionic bond
Hydrogen bond
Forces between polar molecules
Specifically involves hydrogen (H) bound to a more electronegative atom, such as N, O or F,) and an O, N or F of another molecule.
Organic molecules
Hydrocarbon based
i.e Carbon with hydrogen e.g. carbohydrates, CH3OH
Carbon
Single bonding
Double bonding
Triple bonding
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Functional Groups
Specific groups of atoms added to organic molecules Lend specific chemical characteristics to molecule in which group occurs
What charge will the following molecule have in an aqueous environment (aq)?
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Functional Groups
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Figure 2-5
Functional Groups
STRUCTURE
NAME OF COMPOUND
Functional Groups
NAME OF COMPOUND
STRUCTURE
FUNCTIONAL PROPERTIES
EXAMPLE
Functional Groups
Functional Groups
Carboxyl
STRUCTURE Carboxylic acids, or organic acids NAME OF COMPOUND
EXAMPLE Has acidic properties because the covalent bond between oxygen and hydrogen is so polar; for example, Acetic acid, which gives vinegar its sour taste
FUNCTIONAL PROPERTIES
Acetic acid
Acetate ion
Found in cells in the ionized form with a charge of 1 and called a carboxylate ion (here, specifically, the acetate ion).
Functional Groups
Amino
STRUCTURE NAME OF COMPOUND Amines
EXAMPLE
Glycine Because it also has a carboxyl group, glycine is both an amine and a carboxylic acid; compounds with both groups are called amino acids.
Acts as a base; can pick up an H+ from the surrounding solution (water, in living organisms).
FUNCTIONAL PROPERTIES
(nonionized)
(ionized)
Functional Groups
Amide
+
OH
H2N C
Example of Amide: Peptide bond that joins amino acids in a polypeptide as a result of a dehydration reaction
H2O
N C
H
Functional Groups
Sulfhydryl
STRUCTURE Thiols NAME OF COMPOUND
EXAMPLE Two sulfhydryl groups can react, forming a covalent bond. This cross-linking helps stabilize protein structure. Cross-linking of cysteines in hair proteins maintains the curliness or straightness of hair. Straight hair can be permanently curled by shaping it around curlers, then breaking and re-forming the cross-linking bonds.
FUNCTIONAL PROPERTIES
Functional Groups
Phosphate
STRUCTURE NAME OF COMPOUND
Organic phosphates
EXAMPLE
Glycerol phosphate In addition to taking part in many important chemical reactions in cells, glycerol phosphate provides the backbone for phospholipids, the most prevalent molecules in cell membranes.
Contributes negative charge to the molecule of which it is a part (2 when at the end of a molecule; 1 when located internally in a chain of phosphates).
Has the potential to react with water, releasing energy.
FUNCTIONAL PROPERTIES
a) Lipids
Monomer subunits
Carbohydrates
Monosaccharides
Nucleic Acids
Nucleotides
Proteins
Amino Acids
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Organic macromolecules are synthesized by ______________ reactions. a) b) c) d) e) condensation hydrogenation hydrolysis polyhydration transamination
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Breakdown of organic macromolecules occurs by ______________ reactions. a) b) c) d) e) condensation hydrogenation hydrolysis polyhydration transamination
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monomer
monomer
monomer
OH
OH
polymer
H and OH are removed (~water) subunits join into a polymer. i.e. components are dehydrated
Why does a carboxylic acid (carboxyl) functional group behave differently in solution compared to a hydroxyl?
Has TWO electronegative oxygens The Os pull electrons away from the H atom Weakens the bond between O and H H atoms tends to dissociate from the molecule as a hydrogen (H+) ion. Because it donates hydrogen ions, this group is considered acidic Molecules that contain these groups are known as carboxylic acids.
Functional Groups
Figure 2-5
a) Lipids
Monomer subunits
Carbohydrates
Monosaccharides
Nucleic Acids
Nucleotides
Proteins
Amino Acids
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Organic macromolecules are synthesized by ______________ reactions. a) b) c) d) e) condensation hydrogenation hydrolysis polyhydration transamination
Breakdown of organic macromolecules occurs by ______________ reactions. a) b) c) d) e) condensation hydrogenation hydrolysis polyhydration transamination
monomer
monomer
monomer
OH
OH
polymer
H and OH are removed (~water) subunits join into a polymer. i.e. components are dehydrated
Removal of H2O
water
amino acid 1
amino acid 2
polypeptide
Imagesource: http://en.wikipedia.org/wiki/Condensation_reaction
monomer
monomer
monomer
Polymer is split into smaller subunits by adding H and OH (~water) i.e. polymer is hydrolyzed
Imagesource: http://www.biology-books.com/Standard/standard.html
d) Proteins (polypeptides)
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Lipids
Heterogeneous group of molecules
Defined in terms of solubility characteristics (not structural characteristics)
Lipids
Functions include:
- energy storage - membrane structure - signal transduction
Classes of Lipids
Various classes based structure
Fatty acids Triacylglycerols
a.k.a. triglycerides
Figure 3-27
a) Lipids b) Nucleic Acids (polynucleotides) - Biol 214 c) Carbohydrate (polysaccharides) d) Proteins (polypeptides)
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d) Proteins (polypeptides)
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Carbohydrates
Most abundant organic molecules on Earth!
#1: Cellulose produced by photosynthetic organisms #2: Chitin fungal cell walls, exoskeletons of arthropods
Molecular Structure:
Poly-hydroxyls ~one per carbon carbo hydrate = carbon with water Aldehyde or ketone Often have -ose ending - e.g. glucose, sucrose
5 6
galactose
Carbohydrates
Aldehyde
or
Ketone
- carbonyl within molecule
Figure 3-20
- terminal carbonyl
Categories of Carbohydrates
Monosaccharides Mono = one, sacchar = sugar Disaccharides Di = two, sacchar = sugar Polysaccharides Poly = many, sacchar = sugar
Important Monosaccharides
Monosaccharides
Mono = one, sacchar = sugar - simple sugars - generally have a molecular formula that is some multiple of CH2O
Glucose:
- 6 Carbon aldose = aldohexose C6H12O6 -
Important Monosaccharides
Fructose:
- 6 Carbon ketose = ketohexose
C6H12O6
Galactose:
6 Carbon aldose = aldohexose
C6H12O6
Combines with glucose to form lactose (milk sugar) Galactosemia - genetic disorder - afflicted individuals cannot metabolize galactose - high levels of galactose can lead to metal retardation
Important Monosaccharides
Glyceraldehyde & Dihydroxyacetone (DHA): - 3 Carbon sugars = triose Glyceraldehyde = trialdose DHA = ketotriose - Metabolic intermediates Intermediates of both glycolysis pathway and photosynthesis Reversible interconversion (equilibrium!!!)
FYI: DHA is active ingredient in sunless tanning products Combines with different amino acids to form melanoidins (brown polymers)
Important Disaccharides
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Important Disaccharides
Important Disaccharides
Results in GI disturbances
e.g. upset stomach, diarrhea
Management options:
Avoid dairy products Lactase supplements
Not on empty stomach as low stomach pH will denature the enzyme
Important Polysaccharides
poly = many, sacchar = sugar
Important Polysaccharides
Important Polysaccharides
- Structural
25nm
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Figure 3-25
Many animals (including humans) CAN digest starch but NOT cellulose
Enzymes that digest starch (amylases) by hydrolyzing linkages cant hydrolyze linkages in cellulose (requires cellulases) Cellulose in human food passes through the digestive tract as fiber
Some microorganisms use enzymes (cellulases) to hydrolyze linkages in cellulose Many herbivores (e.g. cows, termites) have symbiotic relationships with such microbes
Important Polysaccharides
- structural
Chitin (14) glucosidic linkages of N-acetylglucose amine (GlcNAc) residues
Figure 3-26
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Figure 3-26
N- Acetylglucosamine (NAG)
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Important Polysaccharides
- Structural
Hyaluronic Acid (aka Hyaluronate) Repeating dimer of glucuronic acid (glucuronate) and NAG, linked
via alternating (13) and (14) glucosidic linkages
Prevalent in connective tissue and epithelial tissue
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Before
After!!!
Glucose modifications
Replacement of a hydroxyl group with another functional group
Examples:
NAG = N-acetyl glucose amine
Amine linked to Acetyl
Glucuronic acid
Carboxyl group
d) Proteins (polypeptides)
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Proteins
Polymers of amino acids
IMMENSELY diverse structures/functions Structure Function
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Protein Functions
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Table 3-1
Figure 3-1
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Glycine (Gly or G)
Alanine (Ala or A)
Valine (Val or V)
Leucine (Leu or L)
Isoleucine (Ile or )
Methionine (Met or M)
Phenylalanine (Phe or F)
Tryptophan (Trp or W)
Proline (Pro or P)
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Figure 3-2
Nonpolar amino acids are also referred to as ________________, meaning they are water-_____________.
a) b) c) d)
Serine (Ser or S)
Threonine (Thr or T)
Cysteine (Cys or C)
Tyrosine (Tyr or Y)
Asparagine (Asn or N)
Glutamine (Gln or Q)
Aspartate (Asp or D)
aka. Aspartic acid
Glutamate (Glu or E)
aka. Glutamic acid
Lysine (Lys or K)
Arginine (Arg or R)
Histidine (His or H)
When placed into solution (aq), the amino acids classified as negatively charged behave as _______ and the amino acids classified as positively charged amino acids behave as ________.
a) b) c) d)
Negative
Positive
Aspartate (Asp or D)
Glutamate (Glu or E)
Lysine (Lys or K)
Arginine (Arg or R)
Histidine (His or H)
Aspartate (Asp or D)
Glutamate (Glu or E)
Lysine (Lys or K)
Arginine (Arg or R)
Histidine (His or H)
Functional Groups
Carboxyl or Carboxylic Acid
STRUCTURE Carboxylic acids, or organic acids NAME OF COMPOUND
EXAMPLE Has acidic properties because the covalent bond between oxygen and hydrogen is so polar; for example, Acetic acid, which gives vinegar its sour taste
FUNCTIONAL PROPERTIES
Acetic acid
Acetate ion
Found in cells in the ionized form with a charge of 1 and called a carboxylate ion (here, specifically, the acetate ion).
Please note:
Students are required to memorize the structures of the 20 amino acids Students DO NOT need to memorize amino acid abbreviations
(Would be helpful for you to know, but you will not be required to memorize these for our class).