functions of proteins
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Functions of Proteins. By: Alec Hoover, Katie Klick, and Cory Yerger(14.1-14.4). Functions of Proteins. Structural support Animals have structural proteins. These are chief constituents in skin, bones, hair, and nails. Two important proteins are: Collagen and keratin Catalysis - PowerPoint PPT PresentationTRANSCRIPT
FUNCTIONS OF PROTEINS
By: Alec Hoover, Katie Klick, and Cory Yerger(14.1-14.4)
Functions of Proteins
Structural support Animals have structural proteins. These are chief
constituents in skin, bones, hair, and nails. Two important proteins are:
Collagen and keratin Catalysis
All reactions that take place in living organisms are catalyzed by proteins called enzymes
Without enzymes reactions would be slow and useless
Continued…
Movement Muscle are made up of protein molecules
Myosin and actin Transport
Hemoglobin in the blood carries oxygen from the lungs to the cells and carbon dioxide from the cells to the lungs Move molecules across the cell brain
Continued…
Hormones Many hormones are protein
insulin, erythropoietin, human growth hormone Protection
The body makes proteins called antibodies to counteract foreign proteins
This is one of the major mechanisms used by the body to fight off diseases
Fibrinogen is the protein used in blood clotting
Continued…
Storage Proteins store material
Example: casein in milk and ovalbumin in eggs store nutrients for newborn mammals and birds.
Ferritin: protein in the liver that stores iron. Regulation
Control the expression of genes Regulate the kind of proteins synthesized in a
particular cell Dictate when it is controlled
Continued… A typical cell contains about 9000 different
proteins; the entire human body has 100,000 different proteins
Classified by two major types: Fibrous proteins
Insoluble in water and used mainly for structural purposes Globular proteins
More or less soluble in water and used mainly for nonstructural purposes
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Side Chains Side chains are responsible for the
characteristics and functions of amino acids
Some amino acids have charged side chains EX: Glutamic Acid & Aspartic Acid
Cysteine Two identical cystine monomers make up
cysteine Unique because its side chain ( -SH) can
form disulfide bridges with another cysteine
Charged Amino Acids When an amino acid has an additional
carboxyl group it loses a proton and forms a corresponding carboxylate anion EX: Glutamic Acid Glutamate Side chain is negatively charges at neutral
pH Histidine, Lysine, & Arginine have basic
side chains Lysine & Arginine have side chains that
are positively charges at or near neutral pH
Aromatic Rings Phenylalanine, Tryptophan, & Tyrosine
have aromatic rings in their side chains Allow us to locate and measure proteins
because the aromatic rings absorb strongly
Can be detected using a spectrophotometer
Key precursors to neurotransmitters (substances involved in the transmission of nerve impulses)
Serotonin Tryptophan is converted to serotonin,
calming agent Low levels of serotonin are associated
with depression High levels produce a hyper condition Bipolar disorder can be managed by
controlling levels of serotonin
L-dopa L-Dihydroxyphenylalanine = L-dopa Low levels of L-dopa are involved in
Parkinson’s disease Tyrosine or phenylalanine supplements
increase levels of dopamine because it passes into the brain quickly through brain-blood barrier
Hormones Tyrosine and Phenylalanine are
transformed into norepinephrine and epinephrine, stimulants
Epinephrine is the “Flight or Fight” hormone Causes the release of glucose and other
nutrients into the blood Stimulates brain function
Side Effects Tyrosine & Phenylalanine may have
unexpected effects in some people Some people get headaches from the
phenylalanine in aspartame, artificial sweetener in diet soft drinks
Tyrosine gives some people a morning lift
Tryptophan helps you sleep at night Milk proteins are an aid in inducing sleep
What Are Amino Acids? Contains amino and carboxyl groups.
Structure: (side chain)
What Are Amino Acids? Form chains that make up proteins
20 common amino acids found in nature Called alpha amino acids
Listed on page 303 in figure 14.1
How do we categorize them? Classified into four groups based off of their
polarity. Non-polar Polar But Neutral Acidic Basic
Non-polar side chains are hydrophobic and the side chains of the rest are hydrophilic.
Side chains are responsible for determining both the structure and function of each protein molecules.
What are Zwitterions? Compounds with a positive charge on one
atom and a negative charge on another are known as zwitterions.
Zwitterions Zwitter is a German word meaning “hybrid” Amino acids are zwitterions in a water
solution and in the solid state As the pH is changed in the solution, the
amount of positive and negative charges in the molecules change.
When the pH is at the level where the positive and negative charges are balanced, it is known as the isoelectric point.