Bichemistry Notes KEY
Bichemistry Notes KEY
What is meant by the term biochemistry? __study of compounds and chemical reactions of
living organisms. _______________________________________
You will recall that organisms are made up of 70% water, and that water is an important solvent
in living things. Even though water is found abundantly in organisms, it is an inorganic
compound, meaning that it does not contain carbon. Review where you find water in organisms.
___1) blood, 2) ICF (intercellular fluid) or tissue fluid, 3) cytosol w/in cytoplasm, 4) lymph
fluids _________________________________________________
Besides for the 70% water, organisms are mostly made up of ^simple and complex organic
compounds that contain both carbon and hydrogen. The reason organic compounds are often
large and complex molecules has to do with the properties of the carbon atom. Can you explain
this?
_carbon must form 4 bonds to become stable – because its electron configuration has 4 e- and 4
vacancies in the valence level. It can therefore bond in a variety of 3D configurations with many
different elements. (*recall HONC 1234)
Carbon atoms can join to form long chains, branched chains, or ring structures.
Examples:
Carbon can also form single, double, or triple bonds with other atoms.
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Biochemistry Notes
IMPORTANT BIOLOGICAL ORGANIC COMPOUNDS
The 4 most important types of organic compounds found in living systems are:
1.____carbohydrates____
2.__ _lipids_____
3.____proteins__
4._____nucleic acids___
These organic compounds, along with other important substances that are needed by the body, are called nutrients.
Can you name some other nutrients in addition to these four?
____H2O, vitamins, minerals such as Na+/Cl- (needed for ion balance), Mg2+ (impt for
enzymes), K+ (impt in blood clotting), Zn (insulin component), Fe (hemoglobin component),
trace elements
Cells are three-dimensional structures that are made up of different chemical compounds arranged in various ways.
When you look at a structural formula of a chemical compound, it looks two-dimensional, but in reality there is a
three dimensional structure, similar to the structures you put together in lab. It makes sense that molecules are three-
dimensional if the cells they make up are three-dimensional.
FUNCTIONS OF CARBOHYDRATES
Where is the energy stored in the carbohydrate?__in the bonds between atoms (potential chemical energy)
Kinds of carbohydrates:
1.__monosaccharides (CnH2nOn) – simple sugar – one unit of a carbohydrate) (monomer)
2.___ disaccharides – two simple sugars bonded together (two units = dimer)
3.__polysaccharides – complex sugars (many monomers joined.
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Biochemistry Notes
Examples of monosaccharides:
1.___glucose_____________________________2._______fructose___________________
3.___galactose___________________________
*sweet in taste, polar covalent bonds allow these to dissolve easily in H2O
Take a look at glucose molecule. Its chemical formula is C6H12O6. Now look at fructose. What is
its chemical formula? _______same – C6H12O6__________________________
Glucose and fructose are isomers:
Isomers: ____molecules with the same chemical formulas, but with different structural
formulas. Form leads to function – each will differ in its function.
Notice that galactose is an isomer of glucose and fructose. Because these three monosaccharides
all have different structures, they will have slightly different functions in the cell.
Examples of polysaccharides:
1.__starch – energy storage molecule in plants (stores glucose)
2.___glycogen – energy storage molecule in animals (humans) (stores glucose)
3.___cellulose – “fiber” – makes up plant cell walls.
*4. Add: Others – like chitin in insect exoskeletons & fungi cell walls.
*Not sweet – too big to dissolve in H2O.
*Note, all three of these are composed of glucose monomers.
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Biochemistry Notes
Although starch, glycogen, and cellulose are made of glucose, they have different functions because the
glucose is arranged differently in each molecule, giving each molecule a different overall structure.
Monomer- __a single unit of an organic compound. Can function on its own or be joined
with other similar monomers to form polymers.
Polymer- many monomers bonded together. Large molecules with many different
functions (ex, starch, cellulose, glycogen)
NOTE: The terms monomer and polymer are general terms used to also describe other
compounds, as well as carbohydrates. (*Note: Dimer = 2 monomers bonded such as sucrose)
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Biochemistry Notes
Dehydration synthesis __process of joining monomers chemically by removing water. Smaller
molecules are joined to form larger molecules. Monomerpolymer.__
Example: ___glucose (C6H12O6) + glucose (C6H12O6) maltose (C12H22O11) + H2O__
*These two reactions are not specific for carbohydrates; they are involved in producing
and breaking down fats, proteins, and other organic compounds.
Remember, we cannot produce our own carbohydrates. Only autotrophs can do this, in the
process of photosynthesis. We obtain our carbohydrates in our diet.
What are some good sources of carbohydrates in the diet? __pasta, veggies, fruit, potatoes, dairy,
wheat, grain, corn, rice, cereals. Sweetstarchy. Simple vs. complex carbs.
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Biochemistry Notes
Processing and Utilization of Carbohydrates in Our Bodies
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Biochemistry Notes
What Plants do with the Glucose They Produce
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Biochemistry Notes
LIPIDS
Kinds of lipids:
1.___fats___________________________
______triglyerides._____________________
2.___oils___________________________
3.___waxes___________________________
4.___steroids – cholesterol, testosterone, estrogen ___
5. phospholipids – in cell membrane
What elements are found in lipids? ___carbon, hydrogen, oxygen (not 1:2:1 – much less oxygen)
Function of lipids:
1.__energy storage – gram for gram 2x as much energy compared to carbs – not quickly broken
down_________________________________________________________
2.__insulation & protection of internal organs (adipose = fat tissue)_____________________
3.__structural components of cell membranes – phospholipids ______________________
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Biochemistry Notes
Saturated and Unsaturated Fat
Examples of saturated fats:___butter, animal fat, lard, dairy products, coconut oil.
What makes a saturated fat solid at room temp and an unsaturated fat liquid at room temp?
___ the double bonds in the unsaturated FA’s make the molecules not “fit” together (they have a
slightly “bent” shape) as nicely (saturated are more linear) into a solid repeating structure.
Different melting points.
NOTE: When a fat is unsaturated, such as olive oil, it contains mostly unsaturated fats but it will
contain some
saturated fats.
Phospholipids
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Biochemistry Notes
Function of phospholipids _important structure of cell membrane____________________
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Biochemistry Notes
Processing and Utilization of Lipids in Our Bodies
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Biochemistry Notes
Steroids
Structural characteristics of steroids___4 interlocking carbon rings and other chemical groups
(variable groups_
Types of steroids
1.___cholesterol____________________________vitamin D – aids in calcium uptake ____
2.___sex hormones________
3.___cortisone_______
Characteristics of Cholesterol
1.__found in animal cell membranes (not plants) _
2.___important in synthesis of steroid hormones, testosterone, estrogen__
3.___in excess, can cause plaque formation in blood vessels and contribute to atherosclerosis and
strokes. _
*Note, dietary cholesterol isn’t main source of body cholesterol. Liver makes it from saturated
FA’s that is why they are so bad for you!
PROTEINS
Proteins are some of the largest and most complex biological compounds. Most of an organism
(70%) is made up of water. Most of the 30% that is remaining is made up of protein.
What makes you different from other organisms has a lot to do with the kinds of proteins making
up your body. You will find out later on that the proteins you have are dependent upon the DNA
in your cells. You have more proteins in common with your parents than you do with your
friends, and more in common with your friends than you do with your pets.
There are thousands of different kinds of proteins in the human body, and there are billions of
total proteins in every cell of your body. Proteins take on many different forms and functions in
your body and in all living things. List some different types of proteins, and give an example of
each type:
1.___cell membrane proteins (receptor, transport, channel)_protective antibodies_
2.____structural proteins_____________________enzymes_____
3.____contractile proteins_____
4.____storage___
5.____transport
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Biochemistry Notes
THE STRUCTURE OF PROTEINS
The elements found in protein are: __CHON________________________________
All proteins are made up of smaller molecules called ___amino acids ______________
Therefore, proteins are considered to be polymers, and the amino acids are the monomers.
There are three chemical groups in all amino acids; what are they?
1.____amino group – NH2
2.____carboxyl group -COOH___
3.____R group – variable group off central carbon – hydrogen
Circle these 3 groups in the diagram:
The bond that forms between them is called a _peptide bond (covalent bond betw carboxyl group
of one AA and amino group of next____
When amino acids bond together to form a dipeptide or polypeptide, the process is called
___dehydration synthesis ____________. If you break a peptide down into its separate amino
acids, the process is called ____hydrolysis___
Complete Protein contains all the amino acids which you can’t synthesize on your own
(there’s 8 or so your body can’t make and therefore HAS to take in from food)
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Biochemistry Notes
Examples of amino acids
What do all amino acids have in common? ___amino, carboxyl, central C-H___
How do the amino acids differ from one another? __R group (variable group) _________
Like the 26 letters of the alphabet which, when arranged in different ways can form many
different words, the 20 amino acids, when arranged in different ways and in different numbers,
can form many different types of proteins.
What differs from one protein to another? (below is hw)
1.___# amino acids (length of chain__
2.___types of amino acids (20 types)___
3.___sequence of amino acids__
4. # of polypeptides used to form final protein (some composed of 2 or 3 poly’s)
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Biochemistry Notes
A closer look at the 20 amino acids
Amino acids can be grouped according to the chemical properties of their variable groups.
1. ____nonpolar (hydrophobic)
2. ____polar (hydrophilic)
3. __electrically charged: - (acidic)
4. __electrically charged: + (basic)
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Biochemistry Notes
The Three-Dimensional Structure of Proteins
Proteins, like all organic molecules, have a three-dimensional structure. After the amino acids are
bound by peptide bonds, they interact with each other, causing the molecule to fold up into a
three-dimensional shape. Furthermore, a protein can be made up of one or several polypeptides.
Take a look at the protein hemoglobin. It is made up of 4 polypeptide chains.
Primary structure __single, straight chain of amino acids (straight chain polypeptide)
Secondary structure ___chain folds into helix (coil) due to hydrogen bonding between R groups.
Tertiary structure ____folding of helix into 3-d globular structure due to R group interactions.
Quaternary structure ___only occurs when >1 polypeptide joins to form protein
If just one amino acid is changed in a protein, this will usually result in a change in the protein’s
structure. If the structure is changed, what else may be changed? __function!______________
An example of this occurs in the protein hemoglobin, where one change in the amino acid
sequence in the entire protein results in a disease called sickle-cell anemia.
The function of hemoglobin is to bind to oxygen and carry it throughout the body. Each red
blood cell contains millions of molecules of hemoglobin. If all of the hemoglobin molecules
have an altered shape, and there are millions in each RBC, than the entire structure of the RBC
tends to change into a “sickle” shape. This shape does not allow for easy movement through
capillaries, so organs of the body are often deprived of oxygen.
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Biochemistry Notes
Processing and Utilization of Proteins in Our Bodies
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Biochemistry Notes
Denaturization____loss of proteins secondary, tertiary and/or quaternary structure
What factors might denature a protein? __heat, pH extremes, salt concentr.___
How do these factors denature proteins?
interfere the hydrogen bonding and R-group interactions between one portion of the molecule
and another, so they “unfold”
Why do you suppose that we could die from a temperature above 105o or 106o F?
denatures essential proteins. chem. rxns with enzymes slow or stop.
CHEMICAL REACTIONS IN CELLS: ENERGY AND ENZYMES
All chemical reactions in cells require the use of biological catalysts called enzymes.
Without enzymes, chemical reactions would occur too slowly at the temperatures found in
an organism. Higher temperatures would increase the rate of chemical reactions, but they harm
or destroy the organism.
Characteristics of enzymes:
1.____all enzymes ore protein (organic catalysts)___
2.___help to speed reactions. specific to each reaction. one enzyme one reaction. reactions
speeded a million to over a trillion times faster.
3.___the 3d shape of an enzyme (tertiary or quaternary struct) is specific for the reactants that are
involved in the rxn
4. Enzymes are often named after the substrate on which they act. Many enzymes also have –ase
endings.
Examples: If sucrose is the substrate, __sucrase______________________ is the enzyme.
If a peptide were the substrate, the enzyme would be ____peptidase______________
5. ___Enzymes lower the activation energy (energy required to make rxn go) so rxn is more
efficient and doesn’t hurt cell. (also – not used upup, like stage in theatre)
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Biochemistry Notes
6. How Enzymes Speed Up Chemical Reactions
FORMS OF ENERGY
Energy cannot be created or destroyed, but energy can and does change form. In photosynthesis
and respiration, energy changes from one form into another. Review the energy changes that take
place in these two reactions:
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Biochemistry Notes
ENERGY IN CHEMICAL REACTIONS
All chemical reactions require activation energy.
Activation energy __Energy required to start a reaction – differs from reaction to reaction.
In reactions that do not occur in organisms, activation energy is often in the form of heat. Heat
makes the molecules move faster, so they have a better chance of colliding and reacting. It helps
to destabilize bonds, so they can more easily break, and new bonds in the products can form. If
that much heat were added to cells, the cells would die. The chemical reactions in our cells are
designed to work best at 98.6oF, body temperature. How can we then overcome the activation
energy barrier of chemical reactions so that they can proceed at the relatively low temperature of
98.6oF?
__Enzymes form interactions with substrate(s) at the active site and stress the bonds of the
substrate so less activation energy is needed to break bonds.
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Biochemistry Notes
How do enzymes lower the amount of activation energy needed to start these 2 types of
reactions?
Hydrolysis reactions: __Enzymes bind with substrates (ex. Polymers and water) and stresses
bonds, so that less A.E. is needed.
Synthesis reactions: _ Enzyme brings substrates close together. Enzyme binds with substrates
(dimers or polymers & water) and stresses bonds so that less A.E. is needed.
There are many chemical reactions that take place in cells – as a matter of fact, all cell processes
are a result of chemical reactions. Here we will be looking at two basic types of chemical
reactions: exothermic reactions and endothermic reactions. Both of these types of reactions
require activation energy.
*Energy absorbed to break old bonds. Energy released when NEW bonds form!!
Characteristics of exothermic reactions:
_ Overall or Net release of energy as reactants become products Ex. H2O2 2H2O +
O2 + heat release__
__Reactants have more PE than products. Reactants are less stable than products (easy to
break bonds). Reactants are more organized (complex than products)
_Less energy is needed to start rxn (break bonds) (A.E.) than is released when new bonds
form in products.
Example: __Cell resp. –or-- H2O2 2H2O + O2 -or- hydrolysis such as dipeptide 2
AA’s + H2O_
Note: In organisms, exothermic reactions are also exergonic. These 2 terms are related but
not exactly the same. The difference will be discussed in chemistry class.
Characteristics of endothermic reactions:
___Overall or net input of energy needed for reactants
_Reactants have less PE than products. Reactants are more stable, less
complex/organized than products (hard to break bonds).___
____More (activation) energy is needed to break bonds in reactants than is released when
new bonds form.
Example: __photosynthesis –or- dehydration synth such as amino acid + amino acid
dipeptide + H2O.
Note: In organisms, endothermic reactions are also endergonic. These 2 terms are related but
not exactly the same. The difference will be discussed in chemistry class.
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Biochemistry Notes
Diagram of Exothermic and Endothermic Reactions
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Biochemistry Notes
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Biochemistry Notes