PROTEINS AND AMINO ACIDS Flashcards
In 1838 when Dutch chemist __________first
identified protein as a substance in all living
things, it is unlikely he realized the importance of
his discovery. Proteins shape our lives. Protein
enzymes break down our food into nutrients the
cells can use. As antibodies they shield us from
disease. Peptide hormones carry messages that
coordinate continuous body activity. They guide
our growth in childhood and maintain our bodies
thereafter; they make us each unique.
Johann Mulder
The structural units of proteins—the _______—
are the working currency of protein in body cells.
Amino acids contain carbon, hydrogen, and oxygen
the same three elements that make up
carbohydrates and fats; however, amino acids and
their proteins have the additional element nitrogen.
Protein is about 16% nitrogen. Several amino acids
also contain sulfur.
amino acids
The term _____ ______ tells us they have a dual
nature. The word amino refers to a base or alkaline
substance, so at once we have a contradiction. How
can a chemical substance be both a base and an
acid, and why is this important? Consider the
significance of this fact as we learn more about
amino acids and their roles in the body.
amino acid
is found in all acids, and in solution carries a negative charge.
carbonyl group
contains the essential element nitrogen and in solution carries a positive
charge.
amino group
An attached radical (R) group: The R stands for radical, a general term referring to a group of elements attached to a
chemical compound. In this case it refers to the attached side chains on amino acids; each one is different.
The distinctive side chain on an amino acid gives it a
unique size, shape, and set of properties.
Compare the structure of the two simplest amino acids—glycine and alanine with the larger and more complex amino
acid arginine with its extended carbon chain (R) and three additional amino groups. Twenty different amino acids are
used to build body proteins. Each has the same core pattern but a specific and different side group.
The dual chemical structure of amino acids, including both acid and base groups, gives them a unique amphoteric
nature, meaning that an amino acid can behave as either an acid or a base, depending on the pH of the solution in
which it is found. This makes it possible for amino acids to act as buffers, important in clinical care.
glycine and alanine
Of the 20 amino acids used to build body proteins, nine cannot
be synthesized by the body and must be supplied in food. These
nine amino acids are designated as indispensable (essential)
amino acids.
* Another five of the 20 can be synthesized in the amounts
needed and are termed dispensable (nonessential) amino acids.
The remaining six fall in between and are known as conditionally
indispensable.
* Although the body is able to synthesize the conditionally
indispensable amino acids, it cannot meet the demand when
tissue needs are elevated or the supply of necessary precursors
is inadequate. Arginine is such an amino acid. The quantity that
can be produced in the liver is not sufficient to meet the needs
of the newborn, so additional amounts must be supplied in
food. The concept of dietary essentiality for the indispensable
and conditionally indispensable amino acids is important when
assessing protein quality.
Essential Amino Acids
The dual chemical nature of amino acids, with a base group on one
end and an acid group on the other, enables them to form the
unique chain structure found in all proteins. The end amino group
of one amino acid joins with the end carboxyl group of the amino
acid next to it. This joining of amino acids is called a peptide bond.
Specific amino acids are joined in a particular sequence to form
long chains called polypeptides, and specific polypeptides come
together to form proteins. Polypeptides vary in length from
relatively short chains of 3 to 15 amino acids called oligopeptides
to medium- sized polypeptides with chains of 21 to 30 amino acids
such as insulin. Larger still are complex proteins made up of several
hundred amino acids.
* To build a compact structure, long polypeptide chains coil or fold
back in a spiral shape called a helix. Other proteins form a pleated
sheet held together by strengthening cross-links of sulfur and
hydrogen bonds. Learning more about the structure of body
proteins helps medical researchers develop effective medications
and understand how genes influence disease risk.
Peptide Bond
- This fibrous protein found in muscle is built from chains of 153
amino acids that coil and unfold as needed. Shaped into long
rods, these fibers end in two- headed bundles so that they can
change shape and bend, making it possible to tighten and
contract muscles and then relax them.
Myosin
- This structural protein contains three separate polypeptide
chains that wind around each other to produce a triple helix.
Thus reinforced, collagen is shaped into long rods and bundled
into stiff fibers to do its job of strengthening bone, cartilage,
and skin to maintain body form.
Collagen
This globular protein includes four globin poly- peptide
chains per molecule of hemoglobin. Each chain has
several hundred amino acids conjugated with a
nonprotein, the iron-containing pigment called heme. The
globin wraps around the heme and forms protective
pockets to secure the iron. The iron in heme has a special
ability to bind oxygen, and as part of the red blood cell
delivers oxygen to the tissues and returns carbon dioxide
for excretion via the lungs.
Hemoglobin
is the major plasma protein and has a compact
globular shape. It consists of a single polypeptide chain of
584 amino acids, twisted and coiled into helix structures
held together by disulfide bridges. Albumin serves as a
carrier protein for drugs, hormones, enzymes, and trace
elements. It helps maintain fluid balance by exerting
colloidal pressure in the capillaries that forces the flow of
nutrients and fluids into the cells and the return of fluid and
waste products out of the cells. In serious illness, albumin is
broken down to supply amino acids for the synthesis of new
proteins to meet the body emergency.
Albumin
- Other proteins with special immune
system and the blood protein fibrinogen,
important in blood clotting. Hormones
such as insulin and thyroxin and the
enzymes that regulate our day-to-day
metabolic activities and produce energy
for work are proteins. structural or
metabolic roles include the antibodies of
the
Proteins with Special Roles
Dietary protein supplies the amino acid building blocks for the growth and maintenance of body tissues across the life
cycle. It must furnish amino acids in the appropriate patterns and amounts for efficient synthesis of specific structural
molecules. Although we often consider dietary protein to be most important during growth and development when new
tissues are being formed, protein needs are also important for maintenance and well-being after the growth potential has
been realized.
Growth, Tissue Building, and Maintenance
Every cell in the human body contains protein so a constant supply is needed to
support the expansion of body tissue as an individual grows from a 7-lb infant to a 160-lb man. Protein is especially
important to support the rapid growth occurring in the first years of life when protein deficits can have lifelong effects.
Protein needs escalate approaching the adolescent growth spurt as bone matrix and muscle tissues expand rapidly.
Good quality protein is needed to support fetal growth and the production of milk.
Infancy, childhood, and adolescence:
Following the attainment of full growth and maturity, protein requirements reach a steady state
based on replacing lost cells and worn-out protein molecules. Loss of cells from the skin and gastrointestinal tract; new
cells formed in growth of hair and nails; and formation of enzymes, hormones, and other control proteins constitute
daily protein needs. Individuals who participate in strength training and muscle growth require additional protein.
Protein requirements demand special attention following recovery from serious illness when depleted protein stores
must be replenished.
Adult maintenance:
Methionine assists in the formation of choline, a
precursor of acetylcholine, and tyrosine is used to synthesize the neurotransmitters dopamine and epinephrine;
tryptophan is the precursor of the neurotransmitter serotonin. Age-related decreases in the neurotransmitter
dopamine are associated with Parkinson’s disease, with muscle tremors and rigidity.
- Form neurotransmitters for brain and nerve function5:
Methionine is the precursor of the conditionally indispensable amino acid cysteine, as
well as carnitine and taurine; carnitine transports long-chain fatty acids into the mitochondria for energy
production, and taurine, found in bile salts, also regulates fluid pressure in the eyes.
*Form other amino acids:
Phenylalanine is the precursor of the conditionally indispensable amino acid tyrosine needed to
make thyroxin and epinephrine.
*Form hormones:
Protein is needed to make anti- bodies for the immune system. Protein molecules
referred to as cytokines participate in the acute phase response that brings about alterations in body metabolism
needed to handle the demands resulting from critical illness, burns, or trauma.
*Support immune function: