PROTEINS
LIFE IS AN ORGANIZED SYSTEM OF COMPLEX CHEMICAL REACTIONS
THE FOUR MOST IMPORTANT MACROMOLECULES IN A LIVING SYSTEM ARE:
NUCLEIC ACIDS: Such as DNA and RNA Nucleic Acids store and transfer chemical information needed by the cell.
CARBOHYDRATES Such as glucose and sucrose Carbohydrates provide the energy to the cell to make ATP
Lipids
Lipids Long–term Energy storage molecules and membranes
PROTEINS Proteins control the chemical activity of the cell and provide the structure of the cell
THERE MAY BE AS MANY AS 60,000 DIFFERENT PROTEINS IN THE HUMAN BODY
Some proteins, such as these collagen fibers, give strength to structures in the body
This genetic condition involving extra stretchy collagen is known as Ehlers- Danlos Syndrome
Hair is made of the protein keratin
The protein melanin gives skin the various shades of color
The protein hemoglobin is in red blood cells and transports oxygen to the cells of the body.
Some hormones are proteins, such as insulin which controls the uptake of glucose by the cells
Beta cells produce the hormone insulin and release it into the blood
Cells have insulin receptors transmembrane proteins that are activated by insulin to allow glucose to move into the cell by facilated difussion
If the cells of the pancreas do not produce insulin, then the person has diabetes and must take insulin produced by other organisms
Other proteins called antibodies protect the body from foreign substances
Such as these antibodies attacking a virus in the blood
Muscles are mostly protien
Both of the muscle fibers, actin and myosin, are proteins
Proteins in the cell membrane allow substances to move into and out of the cell
Perhaps the most important proteins in organisms are enzymes.
Enzymes are proteins that control the rate chemical reactions in the cell
Enzymes do not cause a reaction they make the reaction easier to happen
The enzyme amylase in saliva breaks down starches in the mouth
PROTEINS
All proteins are chains of amino acids
Such as the protein insulin, which is two strands of about fifty amino acids in a chain.
There are about 20 different amino acids. Proteins are different because they have different orders of amino acids.
Amino acids have the same basic structure but the side chains are different, giving them different chemical properties
The side- chains of an amino acid is referred to as an R-group
The R-group is in white.
Some R-groups are polar
Some polar groups have stronger positive or stronger negative areas
The primary structure of a protein is the type and order of the amino acids
Amino acids are linked together by peptide bonds
Peptide bonds are another example of dehydration synthesis
Short chains of amino acids are termed Polypeptides
The secondary structure of a protein is the folding of the amino acid chain.
Tertiary structure is the actual folded structure of the protein
Primary structure is the sequence of amino acids
The secondary is the sheet and helix structures that gives the protein rigidity.
The tertiary structure is the folding of the protein to give it shape
The quaternary structure is the final shape of the protein after it is assembled with other polypeptides
The primary structure is the sequence of the amino acids
Amino acids are connected by covalent peptide bonds
SECONDARY STRUCTURE Alpha Helix
The alpha helix sections of trans- membrane proteins often form the channel in facilitated transport proteins, such as this glucose transport protein
Beta sheets give a protein rigidity
Cystine bonds form between the sulfur atoms in the R- group of the cystine
Disulfide bonds are important in determining the tertiary structure
Disulfide bonds form where the amino acid cystine are brought close together
The difference between curly and straight hair is the the number of disulfide bonds between cystine amino acids in the keratin protein
These two proteins are different because they have a different number and a different order of amino acids.
Some proteins have less than 100 amino acids
Most proteins have many hundred amino acids
The shape of the enzyme proteins are essential for their proper function.
A mistake in the hemoglobin protein can cause a condition called sickle cell disease.
Sickle cell disease is caused by one amino acid difference in the 150 amino acids that make up the hemoglobin molecule.
How do the cells make proteins
We eat proteins in our food. In the stomach and the small intestines digestive enzymes break down the proteins into separate amino acids.
In the small intestines the amino acids are absorbed through the villi into the blood vessels of the circulatory system.
The circulatory system carries the amino acids to all parts of the body in the serum of the blood.
In the capillaries amino acids diffuse into the cells.
In the cytosol the amino acids attach to specific transfer-RNA
Each type of t-RNA combines with a specific amino acid
You have to eat 8 of the amino acids, your body can make the rest. These are called the essential amino acids.
RIBOSOME PROTEIN In the cytoplasm of the cells, amino acids are assembled into the correct order to make the right protein
Ribosomes are very small structures in the cytoplasm of all cells including bacteria Proteins are made on the ribosomes
DNA has the information for the correct order of the amino acids to make a working protein
DNA Ribosomes Messenger-RNA carries the information from the DNA in the nucleus to the ribosomes in the cytoplasm
The information is carried to the ribosomes by RNA
RNA is an exact copy of the information for the sequence of the amino acids to make the protein
DNA is made of four different bases connecting the two sides of the spiraling sides.
The order of the four bases are the code for the order of the amino acids in the protein. The four bases are adenine (A), guanine (G), thymine (T) and cytosine (C).
RNA copies the order of the complimentary bases from the DNA
Each three bases of DNA is the code of one amino acid
DNA makes RNA. RNA takes code out of nucleus to the ribosome
The process of making RNA from DNA is called Transcription
Transcription begins when RNA polymerase attaches to a region of DNA called a promoter
The promoter defines the start of a gene, the direction of transcription and the strand to be transcribed
RNA Polymerase binds to the promoter and binds complementary bases until it reaches a stop sequence
The primary RNA molecule is modified and prepared to leave the nucleus.
1. A cap is added to tell the molecule where to attach to the ribosome
2. The introns are removed by enzymes called spliceosomes
3. The mature RNA leaves the nucleus through a nuclear pore
Introns- Sections of “junk DNA” The functions of introns is truly unknown but the thoughts are: -Allow RNA to be spliced together in slightly different orders -Regulate gene feedback -Allow for complexity in organisms without increasing the amount of DNA
Once the RNA has left the nucleus it is taken to the ribosomes
Ribosomes are made of Ribosomal RNA (rRNA) with a variety of proteins and are broken into two subunits
rRNA provides a binding site for the mRNA and the tRNA once binded the large molecule is called a polyribosome
When the mRNA binds to rRNA translation can occur
Translation occurs in three steps: Initiation- The start codon of the mRNA binds to the small subunit of the rRNA, the initiator tRNA binds along with the large subunit
2. Elongation
3. Termination- When the rRNA reaches a stop codon, the polypeptide is released, and the rRNA breaks into its two subunits
As the protein is being made, the first couple amino acids act as a tag to determine where the protein will end up. When the protein is released from the ribosome if needed, it will be taken to the ER and/or golgi for folding, processing, tagging and packaging
Review of RNA How many types? Functions? What does the R mean? What nucleotides make up RNA?
Sickle Cell Disease is caused by a single mutation in the gene for the globin part of the hemoglobin molecule.
A hemoglobin molecule is made of four globin molecules.
A change of one base in the DNA, will change the base in the RNA, which may change the amino acid, which may change the protein.
If the globin molecules in the hemoglobin protein have the mutation, the cell becomes sickle shape.
If only one of the the globin molecules has the mutation, the cell appears normal..
The sickle-cell hemoglobin changes shape when the oxygen is not attached. This change causes a change in the shape of the red blood cell to a crescent shape.
Under low oxygen conditions the cells with mutated hemoglobin become sickle shaped
Round, normal red blood cells easily pass through the junctions of the capillaries
Sickle red blood cells tend to become trapped at these junctions causing swelling and sometimes life threatening clots
Sickle cell disease is a painful conditions but many individuals, such as this professional model, can lead normal lives with precautions.