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Elements of Life
The earths crust contains around 100 or so elements
16 of these are essential for life
Chief Elements Of Ions Trace Elements
Organic Molecules
H hydrogen Na+ Sodium Mn Manganese
C Carbon Mg 2+ Magnesium Fe Iron
N Nitrogen Cl- Chlorine Co Cobalt
O Oxygen K+ Potassium Cu Copper
P phosphorus Ca+ Calcium Zn Zinc
S Sulphur B Boron
Al Aluminium
Si Silicon
V Vanadium
Mo Molybdenum
I Iodine
Elements of Life
The four most common elements in living organisms are:
H, C, O, and N
benzene
octane
http://images.yourdictionary.com/benzene-ring
http://www.green-planet-solar-energy.com/what-is-octane.html
Is polar
Properties of water
Solvent
High heat capacity
High heat of vaporization
High heat of fusion
Density and freezing properties
High surface tension
Is a good reagent
Biologically important functions of
water
Photosynthesis
cellular respiration
The transport of substances from cells to tissues
A good solvent for polar substances and assures the
existence of enzymatic activity.
Temperature Control
Sexual Reproduction
Used as a Lubricant
A mechanism of Support
Reactant
Macromolecules
All living things are made up of four classes of
large biological molecules: carbohydrates, lipids,
proteins, and nucleic acids
These essential fatty acids include the omega-3 fatty acids, required
for normal growth, and thought to provide protection against
cardiovascular disease
Adipose tissue also cushions vital organs and insulates the body
Saturated vs. Unsaturated Fatty Acids
Saturated fats (butter, dairy products, meat) are fats which are evenly filled out with
hydrogen, which remains solid at room temperature. The introduction of double bonds in
the hydrocarbon chain results in the formation of the unsaturated fatty acids (vegetable
oils). The fatty acid with a single double bond is called mono unsaturated fatty acid
(e.g. oleic acid), and if it has multiple double bonds, it’s polyunsaturated (e.g. linoleic
acid). By virtue of their tightly packed structure, the saturated fatty acids increase the
levels of bad cholesterol (LDL) and clog the arteries. On the other hand, the unsaturated
fatty acids increase the levels of good cholesterol (HDL) by taking the LDL to the liver to
be broken down and removed from the body.
Poly unsaturated fatty acids remain liquid at room temp. If it needs to be solidified, it
has to be hydrogenated, or saturated with hydrogen by breaking the carbon double
bonds and attaching hydrogen. The mono unsaturated fats are considered good fats
because of the lower cholesterol content.
Essential fatty acids are poly unsaturated fatty acids that your body can’t manufacture
and, therefore, has to be provided through your diet. It is divided into two groups –
omega 3 and omega 6. Omega 6 is found in corn oil, sunflower oil, and soybean oil,
while omega 3 is present in salmon, trout and tuna. For a healthy diet, concentrate on
mono unsaturated fats like olive oil and essential fatty acids.
http://www.fitday.com/fitness-articles/nutrition/fats/saturated-vs-unsaturated-fatty-acids.html#b
Phospholipids
In a phospholipid, two fatty acids and a phosphate
group are attached to glycerol
The two fatty acid tails are hydrophobic, but the
phosphate group and its attachments form a hydrophilic
head
Phospholipids
When phospholipids are added to water, they self-assemble
into a bilayer, with the hydrophobic tails pointing toward the
interior
The structure of phospholipids results in a bilayer
arrangement found in cell membranes
Phospholipids are the major component of all cell
membranes
Steroids
Steroids are lipids characterized by a carbon
skeleton consisting of four fused rings
Cholesterol, an important steroid, is a component in
animal cell membranes
Although cholesterol is essential in animals, high
levels in the blood may contribute to cardiovascular
disease
Proteins
Proteins account for more than 50% of the dry mass
of most cells
Ionic bonds
Hydrogen bonds
Disulphide bonds
Hydrophobic interactions
•Amino acids are linked by peptide bonds
helix
Hydrogen bond
pleated sheet
Hydrogen bond
http://www.biog1105-1106.org/demos/105/unit1/fibrous_v_glob.html
Figure 5.20b
helix
Hydrogen bond
pleated sheet
strand
Transthyretin
Hydrogen Transthyretin protein
bond polypeptide
Tertiary structure is determined by interactions between
R groups, rather than interactions between backbone
constituents
Hydrogen
bond
Hydrophobic
interactions and
van der Waals
interactions
Disulfide
bridge
Ionic bond
Polypeptide
backbone
Figure 5.20e
Tertiary structure
Transthyretin
polypeptide
Myoglobin is an iron- and oxygen-
binding protein found in the muscle tissue of
vertebrates in general and in almost all mammals. It
is related to hemoglobin, which is the iron- and
oxygen-binding protein in blood, specifically in the
red blood cells.
The only time myoglobin is found in the bloodstream
is when it is released following muscle injury. It is an
abnormal finding, and can be diagnostically
relevant when found in blood
Quaternary structure results when two or more
polypeptide chains form one macromolecule
Quaternary structure
Transthyretin
protein
(four identical
polypeptides)
Figure 5.20h
Collagen
Figure 5.20i
Heme
Iron
subunit
subunit
subunit
subunit
Hemoglobin
Figure 5.20j
Primary Structure refers to the linear sequence of amino acids that make up the polypeptide chain. This sequence is determined by the genetic
code, the sequence of nucleotide bases in the DNA. The bond between two amino acids is a peptide bond. This bond is formed by the removal
of a H20 molecule from two different amino acids, forming a dipeptide. The sequence of amino acids determines the positioning of the
different R groups relative to each other. This positioning therefore determines the way that the protein folds and the final structure of the
molecule.
•The secondary structure of protein molecules refers to the formation of a regular pattern of twists or kinks of the polypeptide chain. The
regularity is due to hydrogen bonds forming between the atoms of the amino acid backbone of the polypeptide chain. The two most common
types of secondary structure are called the alpha helix and ß pleated sheet.
•Tertiary structure refers to the three dimensional globular structure formed by bending and twisting of the polypeptide chain. This process
often means that the linear sequence of amino acids is folded into a compact globular structure. The folding of the polypeptide chain is
stabilized by multiple weak, noncovalent interactions. These interactions include:
◦Hydrogen bonds that form when a Hydrogen atom is shared by two other atoms.
◦Electrostatic interactions that occur between charged amino acid side chains. Electrostatic interactions are attractions between positive and
negative sites on macromolecules.
◦Hydrophobic interactions: During folding of the polypeptide chain, amino acids with a polar (water soluble) side chain are often found on the
surface of the molecule while amino acids with non polar (water insoluble) side chain are buried in the interior. This means that the folded
protein is soluble in water or aqueous solutions.
Covalent bonds may also contribute to tertiary structure. The amino acid, cysteine, has an SH group as part of its R group and therefore, the
disulfide bond (S-S ) can form with an adjacent cysteine. For example, insulin has two polypeptide chains that are joined by two disulfide bonds.
•Quaternary structure refers to the fact that some proteins contain more than one polypeptide chain, adding an additional level of structural
organization: the association of the polypeptide chains. Each polypeptide chain in the protein is called a subunit. The subunits can be the same
polypeptide chain or different ones. For example, the enzyme ß-galactosidase is a tetramer, meaning that it is composed of four subunits, and,
in this case, the subunits are identical - each polypeptide chain has the same sequence of amino acids. Hemoglobin, the oxygen carrying protein
in the blood, is also a tetramer but it is composed of two polypeptide chains of one type (141 amino acids) and two of a different type (146
amino acids). In chemical shorthand, this is referred to as a2ß2 . For some proteins, quaternary structure is required for full activity (function) of
the protein
Source(s):
http://matcmadison.edu/biotech/resources…
Sickle-Cell Disease: A Change in Primary
Structure
3 oxygen.
4
5
subunit 10 m
6
7
3 reduced.
4
5
6 10 m
7 subunit
What Determines Protein Structure?
In addition to primary structure, physical and chemical
conditions can affect structure
tu
Correctly
folded
protein
Polypeptide
Cap
Hollow
cylinder
Chaperonin Steps of Chaperonin 2 The cap attaches, causing 3 The cap comes
(fully assembled) Action: the cylinder to change off, and the
1 An unfolded poly- shape in such a way that properly folded
peptide enters the it creates a hydrophilic protein is
cylinder from environment for the released.
one end. folding of the polypeptide.
Scientists use X-ray crystallography to determine a
protein’s structure
Another method is nuclear magnetic resonance
(NMR) spectroscopy, which does not require protein
crystallization
Bioinformatics uses computer programs to predict
protein structure from amino acid sequences
Figure 5.24
EXPERIMENT
Diffracted
X-rays
X-ray
source X-ray
beam
RESULTS
RNA DNA
RNA
polymerase II
Figure 5.24a
EXPERIMENT
Diffracted
X-rays
X-ray
source X-ray
beam
RESULTS
RNA DNA
RNA
polymerase II