Carbohydrates, proteins, lipids, and nucleic acids
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Transcript Carbohydrates, proteins, lipids, and nucleic acids
Carbohydrates,
proteins, lipids, and
nucleic acids
macromolecules
Organic compound
contain carbon
Carbohydrates
Contain
elements: hydrogen, oxygen, and
carbon
Hydrogen and oxygen are found in the same
ratio as water 2:1
Three types of carbohydrates:
1. Monosaccharides (simple sugars)
Glucose,
fructose, galactose
Have same molecular formula C6H12O6
Differ in their structural formulas
Disaccharides
Two
simple sugars joined together by
dehydration synthesis
Sucrose, maltose
Have same formula C12H22O11
Polysaccharides
Hundreds
of simple sugars bonded together
Cellulose (supporting material found in cell
walls of plant cells)
Starch (plant storage of sugar)
Glycogen (animal storage of sugar, found in
muscle and liver cells)
Dehydration synthesis
(Condensation reaction)
Building up of complex molecules from
simpler molecules, with the release of
water
Hydrolysis
Reverse process, large molecules are
broken down to their building blocks,
with the addition of water
Polymer
Collection of many similar, repeating
units to form a large molecule
Lipids
Fats, oils, and waxes, contain hydrogen,
carbon, and oxygen
Typically consists of a glycerol molecule
bonded to 3 fatty acids known as a
triglyceride
Formed by dehydration synthesis
Saturated fats
Role in heart disease
Have animal origins
Butter, lard, whole milk, and milk products
Solid at rm temp
Saturated with hydrogen atoms which are
attached to each of the carbon atoms
Unsaturated fats
Have at least one carbon to carbon
double bond
Missing hydrogen atoms
Liquid at rm temp
Plant oils such as corn oil, olive oil,
sunflower oil, and fish oils
Proteins
Contain carbon, hydrogen, oxygen, and
nitrogen and in many instances, sulfur
Large polymers of many repeating amino
acid units
20 different types of amino acids
More than 3,000 amino acids in a
protein
Bond between amino acids is called a peptide
bond
A chain of amino acids is a polypeptide
Shape of protein molecule itself depends on
the nature of the attraction between the
different parts of the polypeptide chain
Formed by dehydration synthesis
Polypeptide, not necessarily same
as a protein
Example
Polypeptide would be a strand of yarn
Protein would be a sweater
Shape of protein
Sequence of amino acids determines
proteins shape
Shape determines how protein functions
Function of protein depends on its
ability to recognize and bind to some
other molecules
4 levels of protein structure
1. Primary=sequence of covalently joined
amino acids in a polypeptide (linear)
2. Secondary=bending and hydrogen bonding
of a polypeptide to form helices and pleated
sheets
3. Tertiary=overall shape of polypeptide
4. Quaternary=association between 2 or more
polypeptides
Nucleic acids
Contain carbon, hydrogen, oxygen,
nitrogen, and phosphorus
Largest organic molecules known
Made up of thousands of repeating units
called nucleotides
Nucleotides consist of three parts:
1.
phosphate
2. a five carbon sugar (ribose or deoxyribose)
3. nitrogen base
DNA plays key role in determination of
heredity
RNA important in the synthesis of protein
Enzymes
Organic catalysts, they affect the rate of a
chemical reaction w/out being changed
Can be used over and over again
Protein in nature and specific to their action
Often work with coenzymes which are smaller
and not protein, and are active only with
enzymes
Example
of coenzymes (B-complex vitamins)
How enzymes function:
Enzymes are huge compared to the molecules on which they
interact
Only a small portion of the enzyme functions when it is active,
called the active site
The molecule on which the enzyme acts is called the substrate
They work like a “lock and key”
The name of the enzyme usually has the ending –ase, added to
the stem of the word which is taken from the substrate
Examples:
Enzyme Maltase; substrate Maltose
“
Lipase;
“
Lipids
“
Protease; “
Protein
Factors affecting enzyme action:
pH
Temperature
Depends on enzyme; maltase functions best in a pH of 7; pepsin, found in the
stomach at a pH of1.5-2.2; trypsin, in the small intestine, pH 7.9-9.0
Most function best at body temperature 370 C
Lower temp activity of enzyme decreases
As temp is raised activity increases until a maximum is reached at about 400
C; beyond this point enzyme becomes distorted and enzyme deactivation
occurs
Relative amounts of enzyme and substrate
Amt of enzyme increased, while substrate remains constant; rate of
reaction is increased to a point; after that rate remains constant
Amt of substrate is increased, while concentration of enzymes remains the
same; rate of reaction will increase and will continue up to the point where
every available enzyme molecule is actively involved in the reaction