Transcript Organic Compounds

Lecture #2
Date ______
• Chapter 4~
Carbon &
The Molecular
Diversity of Life
• Chapter 5~
The Structure &
Function of
Macromolecules
• Objectives:
– Chemistry Quiz
– Compare and contrast the
4 groups of organic
compounds
You should know
• Atomic mass, atomic #, valence shells
• Bonds
– Ionic
– Covalent
• Polar (hydrophilic) vs Non-polar (hydrophobic)
– Hydrogen
• Isomer vs Isotope
• Properties of H2O
Practice
1)
2)
3)
4)
7p, 7n, 7e
7p, 8n, 7e
8p, 7n, 7e
9p, 9n, 9e
• How many different
elements are here?
• Which are the same?
• Which has/have a charge
of -1?
• Which has/have an atomic
weight of 15 amu?
• Which has/have 1 valence
e-?
Organic chemistry
• Carbon
-tetravalence
-tetrahedron
-shape determines
function
Organic
Compounds
Hydrocarbons
• Only carbon & hydrogen
(petroleum; lipid ‘tails’)
• Covalent bonding; nonpolar
• High energy storage
• Isomers (same molecular
formula, but different structure &
properties)
– structural~differing covalent
bonding arrangement
– geometric~differing spatial
arrangement
– enantiomers~mirror images
pharmacological industry
(thalidomide – morning
sickness drug)
Testosterone vs Estrogen (fig. 4.8)
Organic compounds
• To build organic compounds you take
hydrocarbon chains and add functional
groups.
• Molecules with the same functional groups
will have similar physical and chemical
properties.
Functional Groups – besides H
Monomer
vs Polymer
Carbohydrates
Monosaccharides – smallest unit
Glucose Isomers
Glycosidic
Linkages
Polysaccharides
Uses of carbohydrates
• Polysaccharides
– Storage:
• Starch~ primary storage molecule for plants
• Glycogen – storage molecule for animals (in liver
and muscles), alpha links, can be broken down by
human enzymes
– Structural:
• Cellulose~ most abundant organic compound;
• Chitin~
exoskeletons; cell walls of fungi;
surgical thread
Simple vs Complex Carbs?
Why are complex carbs better?
1. Weight management – take longer to eat
2. Fiber makes you feel fuller
3. Contain vitamins, minerals, etc.
What happens when you eat too
many carbs?
• Excess carbs stored as fat
• Simple carbs will cause a drastic increase
in glucose – causes a release of insulin
• Insulin then tells your body to store fat
• Complex carbs do not cause a drastic
increase in glucose levels (are broken
down slowly)
Low Carb Diets?
• Carbs are needed to synthesize glycogen which
are needed for effective workouts
• Without glycogen, you cannot burn as much fat
• Body uses fuel in this order (Glycogen, Fat,
Muscle)
• Low calorie diets can make your body burn
muscle which causes a loss in total calorie
burning potential – muscle cells have more
mitochondria)
• Weight comes off because of lost muscle but
comes back as fat (NOT GOOD)
• Ideal amount: 2000 cal diet = 250 g carbs
Lipids – fats, waxes
Triglycerides
– contain C,
H, O
(H:O > 2:1)
Saturated vs Unsaturated
Phospholipids - Amphipathic
Steroids
• Lipids with 4 fused carbon
rings
• Ex: cholesterol:
cell membranes;
precursor for other
steroids (sex hormones);
atherosclerosis
Are ALL Fats Bad?
–Hydrogenating
(adding hydrogen)
unsaturated fats to
make them solid
(peanut butter and
margarine) are just as
unhealthy as
saturated fats
Unhydrogenated Peanut Butter
• Men need 4-7% body fat
• Women need 9-16% body fat
• Going below these
percentages is harmful since
your body can’t perform all its
normal functions
Good Things About Fat
• More energy than carbs or
proteins
• Helps absorb Vitamins A, C,
etc.
• Healthy skin
• Gives us fatty acids for
growth
The Good – Omega-3 Fats
• Lower blood
pressure
• Decrease risk of
heart attack
• Protect against
irregular
heartbeats
How much should you eat?
YUM!
• You should consume 20 to
30% of your total calories from
fat
• No more than 10% should be
saturated fats
Too much or too little
can be a health risk!
Nucleic
Acid
Proteins
Amino Acids/Side Chains
–Nonpolar – contain –CH2 or
–CH3 (Hydrophobic)
–Polar uncharged – Contain
O or only –H (Hydrophilic)
• Ionizable – acid (R groups are negative)
or base groups (R groups = +)
Peptide Bonds/Polypeptide
Primary
Structure –
amino acid
sequence
determines the
protein
-If you switch 2
amino acids, you
get a whole new
protein
Amino acid substitution – 1 out of
600 amino acids
Secondary
Structure –
alpha helix &
beta pleated
sheet
Tertiary
Structure
Quaternary Structure – 2 or more
polypeptides bond together
Protein Folding Animation
• http://intro.bio.umb.edu/111112/111F98Lect/folding.html
• http://intro.bio.umb.edu/111112/111F98Lect/folding.html
AP LAB 2
– Pre-Lab
Warm-up
- Have out your organic compounds WS – we will
go over it
1. What bonding is associated with the following:
– Primary structure of protein?
– Secondary?
– Tertiary?
2. What 2 main functions do proteins provide your
body?
3. What four things does a amino acid have
(structure)?
4. What is the smallest unit of a nucleic acid?
What we’ve covered the last few
days
• Organic compounds – carb, lipid, protein,
nucleic acid
– Monomer, function, elements, examples
– Able to recognize structural/molecular
formulas
• Enzymes
– Protein folding
– Characteristics
– Environmental factors affecting rate (lab)
– Regulation (end of class today)
Homework
• Study for test
• Internet review – not for a grade
• No Quiz tomorrow – canceled
– Quizzes – drop 1 per 9 weeks
Protein Folding
Inactive
Active
Chemical Reactions/EA
• Metabolism – all chemical reactions in a
biological system
• Catabolism – breakdown of substances
• Anabolism – formation of new products
Induced Fit
Induced Fit
Anabolic Enzyme
Catabolic Enzyme
Enzymes
•
•
•
•
•
Bind to substrate (molecule it acts on)
Are specific (binds to certain substrate)
Has active site (where substrate binds)
Are reusable
Are affected by temperature and pH
Enzyme Animations
• http://highered.mcgrawhill.com/sites/0072495855/student_view0/
chapter2/animation__how_enzymes_work.
html
• http://highered.mcgrawhill.com/sites/0072507470/student_view0/
chapter25/animation__enzyme_action_an
d_the_hydrolysis_of_sucrose.html
• http://www.phschool.com/science/biology_
place/labbench/lab2/binding.html
Go over Quiz
Finish Enzyme Lab
• Safety Goggles – pH lab group,
temperature group when heating
• Whiteboard – data while you are finishing,
be ready to explain data after lab
Enzyme Lab Conclusion
• Rate of reaction is determined by
measuring the disappearance of substrate
or the accumulation of product
• Rate of reaction is the slope of the linear
portion of the graph
• Reaction rate is affected by pH, substrate
conc., enzyme conc., temperature, and
ionic con.
Conclusions
• Enzymes have optimum pH,
temperature, and salt concentrations
that they work in
• General rules
– Temp
• Lower the temp, the slower the molecules
collide – slower the reaction rate
• Higher the temp, the faster the molecules
move around – faster the reaction rate
• Too high a temperature (60-70 C) – protein
denatures – reaction doesn’t occur
• pH – too high or too low the H+ or OH –
ions react with the amino acid side chains
(R groups) – improper folding occurs –
reaction slows
• Salt conc. – too much or too little causes
improper folding of protein
• Substrate concentration – lower the
substrate conc., the slower the reaction
• 6. After an enzyme is mixed with its substrate, the amount of
product formed is determined at 10-second intervals for 1
minute. Data from this experiment are shown below:
Time (sec)
0
10 20 30 40 50 60
Product formed (mg) 0.00 0.25 0.50 0.70 0.80 0.85 0.85
• What is the initial rate of this enzymatic reaction? Show your
calculation.
.025 mg/sec
• What is the rate after 50 seconds? Show your calculation. Why
is it different from the initial rate?
.02125/sec (substrate is running out)
Factors
Affecting
Enzyme
Activity
Cofactors/Coenzymes – other
molecules that aid in enzymatic
function (can bind along with the
enzyme)
ATP/Energy
Coupling
Enzyme Regulation –
Inhibition/Activation
Allosteric Regulation
Enzymes –
Active and
Allosteric
Sites
Enzyme Animations
• http://www.northland.cc.mn.us/biology/biol
ogy1111/animations/enzyme.swf
• http://bcs.whfreeman.com/thelifewire/conte
nt/chp06/0602001.html
Feedback
Inhibition