Protein play countless roles throughout the biological world.

Some transport nutrients throughout

the body. Some help chemical reactions happen at faster rates. Others build the structures of
living things.
Five Main Function of Proteins
-Building Tissues and Muscles
-Hormone Production
–Enzymes
-Immune Function
-Energy

Despite this wide range of functions all proteins are made of the same building blocks called
amino acids.
Amino acids are organic compounds made of carbon, hydrogen, nitrogen, oxygen and some
contains sulfur.
Selenocysteine is the only amino acid that contains a selenium atom. These amino acids form an
amino group, a carboxyl group and a side chain all attached to a central carbon (alpha carbon).
The side chain determines the amino acid’s properties and it is the only part which varies amino
acids to other amino acids.
Hydrophobic amino acids have carbon-rich side chains which don’t interact well with water.
Hydrophilic or polar amino acids interact well with water. Charged amino acids interact with
oppositely charged amino acids or other molecules.
Enzymatic Protein- are enzymes that can speed up chemical reaction to your body.
Structural proteins are fibrous proteins. The most familiar of the fibrous proteins are probably the
keratins, which form the protective covering of all land vertebrates: skin, fur, hair, wool, claws,
nails, hooves, horns, scales, beaks and feathers. Equally widespread, if less visible, are the actin
and myosin proteins of muscles tissue. Another group of fibrous structural proteins are the silks
and insects fibers. In addition, there are the collagens of tendons and hides, which form
connective ligaments within the body and give extra support to the skin where needed.
Transport Protein- are proteins that transport substances across biological membranes. Transport
proteins are found within the membrane itself, where they form a channel, or a carrying
mechanism, to allow their substrate to pass from one side to the other.
Two types of transporter proteins:
1. Channel proteins
 2. Carrier proteins

Defensive proteins are know as antibodies and are found in the immune system. The defensive
proteins, also known as antibodies are produced by the body to fight diseases and prevent injury.
Regulatory Protein (gene-regulatory protein) is any protein that influences the regions of a DNA
molecule that are transcribed by RNA polymerase during the process of transcription.
These proteins, which include transcription factors, therefore help control the synthesis
of proteins in cells. "regulatory protein."
Regulatory Protein is made by:
A. DNA TRANSCRIPTION
Transcription is the first step of gene expression. During this process, the DNA sequence of a
gene is copied into RNA.
Before transcription can take place, the DNA double helix must unwind near the gene that is
getting transcribed. The region of opened-up DNA is called a transcription bubble.
Transcription uses one of the two exposed DNA strands as a template; this strand is called
the template strand. The RNA product is complementary to the template strand and is almost
identical to the other DNA strand, called the nontemplate (or coding) strand. However, there is
one important difference: in the newly made RNA, all of the T nucleotides are replaced with U
nucleotides.
The site on the DNA from which the first RNA nucleotide is transcribed is called the +1+1plus,
1 site, or the initiation site. Nucleotides that come before the initiation site are given negative
numbers and said to be upstream. Nucleotides that come after the initiation site are marked with
positive numbers and said to be downstream.
If the gene that's transcribed encodes a protein (which many genes do), the RNA molecule will
be read to make a protein in a process called translation.
Step 1: INITIATION
To begin transcribing a gene, RNA polymerase binds to the DNA of the gene at a region called
the promoter. Basically, the promoter tells the polymerase where to "sit down" on the DNA and
begin transcribing.
Step 2: ELONGATION
Once RNA polymerase is in position at the promoter, the next step of transcription—
elongation—can begin. Basically, elongation is the stage when the RNA strand gets longer,
thanks to the addition of new nucleotides.
During elongation, RNA polymerase "walks" along one strand of DNA, known as the template
strand, in the 3' to 5' direction. For each nucleotide in the template, RNA polymerase adds a
matching (complementary) RNA nucleotide to the 3' end of the RNA strand.
The RNA transcript is nearly identical to the non-template, or coding, strand of DNA. However,
RNA strands have the base uracil (U) in place of thymine (T), as well as a slightly different sugar
in the nucleotide. So, as we can see in the diagram above, each T of the coding strand is replaced
with a U in the RNA transcript.
Step 3: TERMINATION
RNA polymerase will keep transcribing until it gets signals to stop. The process of ending
transcription is called termination, and it happens once the polymerase transcribes a sequence of
DNA known as a terminator.
After termination, transcription is finished. An RNA transcript that is ready to be used in
translation is called a messenger RNA (mRNA). In bacteria, RNA transcripts are ready to be
translated right after transcription. In fact, they're actually ready a little sooner than that:
translation may start while transcription is still going on!
mRNAs are being transcribed from several different genes. Although transcription is still in
progress, ribosomes have attached each mRNA and begun to translate it into protein. When an
mRNA is being translated by multiple ribosomes, the mRNA and ribosomes together are said to
form a polyribosome.

B. RNA TRANSLATION
Translation has pretty much the same three parts, but they have fancier names: initiation,
elongation, and termination.
Step 1: Initiation ("beginning"): in this stage, the ribosome gets together with the mRNA and the
first tRNA so translation can begin.
translation initiation goes like this: first, the tRNA carrying methionine attaches to the small
ribosomal subunit. Together, they bind to the 5' end of the mRNA by recognizing the 5' GTP cap
(added during processing in the nucleus). Then, they "walk" along the mRNA in the 3' direction,
stopping when they reach the start codon (often, but not always, the first AUG).
Step 2: Elongation ("middle"): in this stage, amino acids are brought to the ribosome by tRNAs
and linked together to form a chain.
Our first, methionine-carrying tRNA starts out in the middle slot of the ribosome, called the P
site. Next to it, a fresh codon is exposed in another slot, called the A site. The A site will be the
"landing site" for the next tRNA, one whose anticodon is a perfect (complementary) match for
the exposed codon.
Once the matching tRNA has landed in the A site, it's time for the action: that is, the formation of
the peptide bond that connects one amino acid to another. This step transfers the methionine
from the first tRNA onto the amino acid of the second tRNA in the A site.

Step 3: Termination ("end"): in the last stage, the finished polypeptide is released to go and do its
job in the cell.
Termination happens when a stop codon in the mRNA (UAA, UAG, or UGA) enters the A site.
Stop codons are recognized by proteins called release factors, which fit neatly into the P site
(though they aren't tRNAs). Release factors mess with the enzyme that normally forms peptide
bonds: they make it add a water molecule to the last amino acid of the chain. This reaction
separates the chain from the tRNA, and the newly made protein is released.
Storage proteins serve as biological reserves of metal ions and amino acids, used by organisms.
They are found in plant seeds, egg whites, and milk. Ferritin is an example of a storage protein
that stores iron. Iron is a component of heme, which is contained in the transport protein,
hemoglobin and in cytochromes.