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MOLECULARBIO LESSON 3 Proteins and Mutation Edited
MOLECULARBIO LESSON 3 Proteins and Mutation Edited
Differ from the parent amino acids in that Differs from tyrosine in that it has an extra
they hydroxyl groups on their side chains. Iodine-containing aromatic group on the side
chain.
Found only in a few connective tissue
proteins, such as collagen. Produced only in the thyroid gland, formed
by posttranslational modification of tyrosine
residues in the protein thyroglobulin
ESSENTIAL NONESSENT
IAL
Arginine° Plays an important role in cell Alanine Simplest of the amino acids and its
division, the healing of wounds, involves in the energy-producing
stimulation of preotein synthesis, breakdown of glucose.
immune function, and the release of
hormones Plays a major role in the transfer of
nitrogen from peripheral tissue to the
liver.
Histidine Direct precursor of histamine, one of Asparagine one of the principal and frequently
the proteins invloved in the immune and the most abundant of the amino
response acids involved in the transport of
nitrogen.
Important source of carbon atoms in
the synthesis of purines, one of the Major fnx: convert one amino acid
two groups of nitrogen bases that into another via amination and
make up DNA and RNA transamination.
Helps manufacture red and white Required by the nervous sytem and
blood cells and helps to protect the plays an imporatnat role in the
body from heavy metal toxicity sythesis of ammonia.
Isoleucine Helps maintain, heal, and repair Aspartate plays a vital role in metabolism
muscle tissue, skin, and bones. during construction of other amino
acids and metabolites in the citric
Needed for hemoglobin formation acid cycle.
Leucine Second most common amino acid Cysteine may be essential for infants, elderly,
found in protein beside glycine and individuals with certain
metabolic diseases or malabsorption
Boosts the healing of muscle, skin, syndromes.
and bones with the help of valine
and is isoleucine Potentially toxic and is catabolized in
Aids in recovery from surgery and the gastrointestinal tract and blood.
lowers blood glucose levels
Cysteine is absorbed during digestion
Necessary for the optimal growth of as cystine, which is more stable in
infants and for nitrogen balance in the gastrointestinal tract.
adults
Methionine Important amino acid that helps to Glutamate linked to epileptic seizures.
initiate translation of messenger
RNA by being the first amino acid A neurotransmitter, is important in
incorporated into the N-terminal the metabolism of sugars and fats,
position of all proteins and aids transporting potassium into
the spinal fluid.
Phenylalanin Promotes alertness and vitality, Glutamine Most important amino acid in the
e elevates mood, decreases paim, aids body, being involved in more
memory and learning, and is used to mtaboliv processes than any other
threat arthritis and depression. amino acid.
Valine A constituent of fibrous proteins in Serine Needed for the proper metabolism of
the body. fats and fatty acids and plays an
important role in the body’s synthetic
Needed for muscle metabolism and pathways for pyrimidines, purines
coordination, tissue repair, and (making it important for DNA and
maintenance of nitrogen balance. RNA fxn), creatine, and porphyrins.
Is a covalent bond between the carboxyl group of one Fxns: Hormonal action: OXYTOCIN &
amino acid and the amino group of another amino VASOPRESSIN
acid.
Neurotransmission: ENKEPHALUS
Antioxidant activity: GLUTATHIONE
PROTEIN STRUCTURE
CLASSIFICATION OF PROTEIN
BASED ON SHAPE
1. FIBROUS- a protein whose molecules have an elongated shape with one dimension with one
dimension much longer than the others.
FIBROUS PROTEIN:
2. GLOBULAR- a protein whose molecules have peptide chains that are folded into spherical or
globular shapes.
GLOBULAR PROTEIN:
KERATIN Found in wool, feathers, hooves, silk, and fingernails.
ELASTIN BASED
Found in blood vessels andON FUNCTIONS
ligaments.
DEFENSE Immunoglobulins or antibodies are central to the functioning of the body’s immune
PROTEINS system. They bind to foreign substances, such as bacteria and viruses, to help
combat invasion of the body by foreign particles.
TRANSPORT HEMOGLOBIN-carries oxygen from the lungs to other organs and tissues.
PROTEIN TRANSFERRIN- carries iron from the liver to the bone marrow.
HIGH AND LOW DENSITY LIPOPROTEINS- carriers of CHOLESTEROL in
the bloodstream.
MESSENGER Proteins that transmit signals to coordinate biochemical processes between different
PROTEIN cells, tissues, and organs.
(e.g. insulin, growth hormone and glucagon)
CONTACTILE -Proteins are necessary for all forms of movement.
PROTEIN -Muscles are composed of filament-like contractile proteins that, in response to
nerves stimuli, undego conformation changes that involve contraction and extension.
-Actin and myosin are examples of such proteins
-Human reproduction depends on the movement of sperm. Sperm can “swim”
because of long flagella made up of contractile proteins.
STRUCTURA -proteins confer stiffness and rigidity to otherwise fluid-like biochemical systems.
L -collagen is a component of cartilage.
PROTEIN -a keratin gives mechanical strenghth as well as protective covering to hair,
fingernails, feathers, hooves, and some animal shells.
TRANS- Help control the movement of small molecules and ions thru the cell membrane.
MEMBRANE
PROTEIN
-proteins bind (and store) small moleculesfor future use.
STORAGE -FERRITIN- an iron storage protein, which saves the iron for use in the
PROTEIN biosynthesis of new hemoglobin molecules.
-MYOGLOBIN- an oxygen-storage protein present in msucle: the oxygen so stored
is a reserve oxygen source for working msucle.
REGULATOR -act as sites at which messenger molecules, including messenger proteins such as
Y insulin, can bind and thereby initiate the effect that the messenger “carries”.
PROTEIN
-often the molecules that bind to enzymes (catalytic proteins), thereby turning them
“on” and “off”, and thus controlling enxymatic action.
NUTRIENT -proteins are particularly important in the eraly stages of life, from embryo to infant.
PROTEIN -CASEIN- found in milk
-OVALBUMIN- found in egg white
GLYCOPROTEINS
A protein that contains carbohydrates or carbohydrate derivatives in addition to amino acids.
Includes several very important substances; two of these,COLLAGEN and
IMMUNOGLOBULINS.
Types: Collagen
Immunoglobulin
Collagen Immunoglobulin
Presence of carbohydrate units attached by Glycoprotein produced by an organism as a
glycosidic linkages to collagen at its 5- protective responnse to the invasion of
hydroxylysine residues causes collagen to be microorganisms or foreign molecules.
classified as a glycoprotein.
TYPES: G A M B E
Example: breast milk secretion colostrum
(IgA)
````
LIPOPROTEINS
Conjugated protein that contains lipids in addition to amino acids.
Major function of such proteins is to help suspend lipids and transport them through the bloodstream.
Plasma Protein – lipoprotein that is involved in the transport system for lipids in the bloodstream.
Four major classes of Plasma Proteins;
1. Chylomicrons – their function is to transport dietary triacylglycerols from the intestine to the
liver and to adipose tissue.
2. Very-Low-Density Lipoprotein (VLDL) – their function is to transport triacylglycerols
synthesized in the liver to adipose tissue.
3. Low-Density Lipoprotein (LDL) – their function is to transport cholesterol synthesized in the
liver to cells throughout the body.
4. High-Density Lipoprotein (HDL) – their function is to collect excess cholesterol from the body
tissues and transport it back to liver for degradation to bile acids.
Protein Denaturation
Partial or complete disorganization of protein’s characteristic three-dimensional shape as a result of
disruption of its secondary, tertiary and quaternary structural interactions.
INITIATION
ELONGATION
TERMINATION
MUTATIONS
Changes in nucleotide sequences of DNA
May occur in somatic cells or in gametes
Chemical and UV radiation can cause mutation
Can be repaired by enzymes
Classes of Mutations
1. Spontaneous Mutation
Happens during DNA replication or incorporation of incorrect nucleotide in a replicating DNA.
Occurs naturally during DNA replication where changes in DNA sequences happen.
2. Induced
Mutation
Caused by mutagens which are an environmental factor that changes the DNA sequence.
Examples; UV lights, X-rays, Gamma rays etc.
Types of Mutations
1. Chromosome Mutation
Involves changing the structure of a chromosome.
Involves deletion and addition of the part of a chromosome.
Five Types
Deletion – due to breakage, a piece of chromosome is lost.
Inversion – a segment of a chromosome breaks and flips and reattached again to the
segment.
Translocation – process where part of the chromosome transfer to another chromosome.
Nondisjunction – happens when chromosome fails to separate during meiosis. Causes
the gametes to have many or few chromosomes.
Duplication – happens when the gene sequence is repeated.
2. Gene Mutation
Change in nucleotide sequence of a gene involving single nucleotide due to copying, errors,
chemicals, viruses etc.
Types
Point Mutation – involves 3 types of mutation in a single nucleotide in a gene insertion,
deletion and substitution.
Substitution – one base pair is replaced by different base pair.
Insertion – changes the DNA sequence by adding one or more nucleotides to the gene.
Deletion – changes the DNA sequence by removing at least one nucleotide in a gene,
Frameshift – this is due to inserting or deleting one or more nucleotides. It drastically
alters the protein and built incorrectly
3. Morphological Mutation
Generated a visible morphological alterations.
Examples; size, shape and color
4. Lethal Mutation
Fatal in nature
Causes death of an individual
5. Conditional Mutation
Normal under one condition (permissive) but abnormal under another (restrictive)
Useful in studying processes such as development and DNA replication.
6. Biochemical Mutation
Mutation is due to loss or of some biochemical means or nutritional function in cell.