EVOLUTION OF PROTEINS
What
are proteins?
Proteins are polymers or combinations of various amino
acids called peptides when they are bound in a chain. A tri-peptide is composed of three amino acid
residues, polypeptides of multiple ones; proteins have residues numbering in
the hundreds and more. Each amino acid
incorporates a nitrogen atom in its structure at the site where it can be
combined with the acid-like part of another amino acid, leaving similar
junction sites on the resulting molecule so longer chains can be produced. Further linkages via side chains can yield a
great variety of shapes.
Why
are proteins important?
They are the key to much of the structure and
function of an organism. Many of them
are common to other distantly related species.
Some are unique to a species and even individuals or a subgroup of a
species.
The proteins of our body have great diversity based
on variations in the sequence and the resultant structure. Enzymes are proteins useful in aiding
chemical processes of the body. Insulin
is a protein type hormone. Enzymes and
hormones vary greatly in size but are typically much smaller than proteins used
for structural purposes. Both enzymes
and hormones typically have their activity based on a peculiar aspect of their
structure, often just a small portion of the molecule – the active site.
Hormones cause cells or organs, in various specific
locations away from the sites of hormone production, to do their jobs. Enzymes typically enable a chemical reaction
to occur with minimal energy expenditure and can do so repeatedly. Cooking deactivates enzymes and prevents
decomposition until other organisms digest or invade the cooked food.
Myosin and
actin are two major proteins of muscle and each has a filament type structure. Large
bundles of myosin slide past smaller bundles of actin and cause muscles to shorten
and do their work. Opposing muscles
contract to cause the extension of an opposing relaxing muscle by force applied
through the mechanics of the skeleton or tissue fluidity.
What
evolutionary affects did the nitrogen atom of amino acids have?
When an amino acid or peptide is broken down the
nitrogen atom can be released as an ammonium molecule, a toxic substance if
concentrations build up in the body.
Most carbohydrates and lipids do not contain nitrogen so their residue,
after use for energy, is carbon dioxide and water. So is much of the protein but the ammonia
cannot be passed into the air from fluid in the lungs very effectively. Aquatic animals were able to accomplish much
of the early evolution of life without needing special organs to dispose of
nitrogenous waste. The ammonia could
diffuse from the body surface or gills into water where it would be useful for
plants.
As organisms got larger those that could package
ammonia into less toxic forms had an advantage.
Urea and uric acid are two of the substances that were selected for most
successful animals. Urea is soluble in
water but non-toxic; it is the major compound containing nitrogen that is
excreted by the mammalian kidney. Uric
acid is toxic but not very soluble and it is the main product produced by
degradation of adenine and guanine from the nucleic acids, DNA and RNA.
Biochemical processes in animals are varied in their potential to make
various conversions of nitrogenous wastes.
Along the way, kidneys became more and more important for regulating
levels of nitrogenous wastes in the blood as well as salt and water balance
while retaining nutrients.
Uric acid made it possible for shelled eggs of
animals to evolve for life on land. It
could accumulate in the egg without poisoning the embryo. That made it possible for reptiles to lay
their shelled eggs on land. Birds
continued the egg-laying process, as did early mammals (the platypus and
echidna still do). Eventually placental
mammals developed and transferred nitrogenous wastes from the fetus to the
mother for elimination by her kidneys.
Why didn’t birds go that route? Probably it has weight reducing value for
flight. It’s so important that only one
ovary develops in a female bird, probably enabling larger eggs to be laid that
can develop to greater maturity. You can
probably think of the survival advantage a mammal has from being able to takes
its internal young with it and not be bound to a nest location and its hazards.
Proteins
and the pharmaceutical industry
Hormone and enzyme activity must be well regulated
by the body for health. Too much or too
little function can be detrimental to health.
Some classes of drugs are designed to have function like those items in
the body. They can supplement the body’s
product or interfere with its function as needed to get the correct
balance. The critical aspect is getting
an active site incorporated in a non-toxic molecule that can go to the needed
area. Alternatively, a toxic molecule
designed for attraction to a cancer cell or overactive gland might be helpful.
Trial and error methods are being replaced by
analysis of molecular structure for duplication of active sites in a synthetic
substitute. The active site in some
cases is not dependent upon the chemical nature as much as the physical shape
of the portion of the molecule. Other
parts of the molecule may affect some part of the process so clinical trials
are needed to verify safety and effectiveness.
Unfortunately all possible interactions, with systems
of the body at all stages of function and development, breakdown products and
their role in the environment, and other possible hazards cannot be
foreseen. But we hope care in the
process can minimize the hazards.
The computerized process of designing molecules
based on fit with some portion of hormones, enzymes, cell membrane receptors or
other entities is a likely source of valuable products. But individuals and/or conventional research
teams cannot be replaced as easily for less conventional and serendipitous
discovery.
Joseph G. Engemann April 30, 2014