Pogue 8.1, Cheri scr ofthe 20 standard aminoacids pls Selenccycoine,
Proteins
Proteins are the most
abundant organic ‘compounds
found in any living organism, |
The name protein came from the
Greek word proteos meaning
“first place.” It is a biological
polymer constructed from amino
acids as its monomer. Proteins
are important in the structure
of the cells; they serve as gene
activators, membrane receptors,
transporters, clotting factors, et
There are seven major classes of |
proteins which include: j
1, Structural protein — found
in the hair of mammals; fiber
that makes up the tendons |
and ligaments i
2. Contractile protein-protein’ _
that provide muscular
movement
3. Storage protein — such as
ovalbumin, the main substance
of egg whitensive protein - includes antibodies that promote protection against foreign bodies
sport protein — includes hemoglobin, the iron-containing protein in the blood that
sports oxygen from the lungs to the other parts of the body
'al protein - such as hormones which help coordinate body activities
IZYMe ~ serves as the chemical catalyst that changes the rate of chemical reactions
There are 20 amino acids that arein the human body (Figure 5.1), We are capable of making
Of these amino acids but the other nine must be consumed. Thus, these nine amino acids are
d essential amino acids. The essential amino acids ae histidine, isoleucine, leucine, lysine,
Honine, phenylalanine, threonine, tryptophan, and valine. Each amino acid has a central
ine group. Water is released as a by-
uct during this process.
ur Structures of Protein
The complex configuration of a
Btein dictates its function (Figure 5.2)
primary structure of @ protein shows
sequence of amino acids forming
peptide chains. The primary structure
tached together by covalent or peptide
\ds. This process is done during the pon
of protein biosynthesis ortransiation, Toray structure
structure is determined by the gene
sponding to the protein. During protein
thesis, aspactc sequence of nucleotides Syurstprasinnes
1e DNA is transcribed into mRNA, which ewe 52.
n read by the ribosome in a processcalled translation. Protein sequences are unique for each type of protein. This, later on, defing,
the structure and function of the protein. The amino acid sequence can then form its seconda,
structure, a highly regular local sub-structure that can take the form of an alpha helix or a ber,
strand. These structures are defined by hydrogen bonds between the main chain peptide groups
(a) Pay snenee chal ae
gure. tharatn a pinay to ater leon cf emogain. Content amin acid canbe aad
te rece scandy ata, and quate pron stuces Ihc, eosin coin home units.
‘The alpha- or beta-sheets can then transform tots tertiary structure, which pertains to the
‘overall 30 shape of a polypeptide by a pattern of folding driven by the non-specific hydrophobic
interactions. The alpha-helices and beta-sheets are folded into a compact globule. Quaternary
structure is the arrangement of multiple folded protein or coiling protein molecules in a mult-
subunit complex. An example is the oxygen-transporting molecule hemoglobin which has four
subunits (Figure 5.3). Another example of @ common quatemary protein is collagen fibers.
Role of Proteins
Humans need to consume protein to maintain a source of nitrogen that is used by
the body in the production of new cells and the formation of new compounds. Proteins ar@nade up of smaller units called amino acids. There are 20 different types of amino acids that
an assemble in different configurations to form longer chains. The sequence of amino acids
_gctates the function ofthe protein. This makes up parts of the cellular components and the cell
membrane, thus, implying that protein is found in every cell in the human body. Some proteins
help in maintaining the fluid balance in the blood and other tissues, as well as maintain the acid-
base balance. The nine essential acids that the human body does not synthesize are histidine,
izoleucne, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. Food
that contain these nine essential acids in roughly equal proportions are called complete proteins.
Complete proteins mainly come from animal sources, such as milk, meat, and eggs.
Perhaps some of the most important proteins in the body are enzymes that aid in the
chemical reactions occurring in each cell and are known to assist in DNA replication, transcription,
and vanslation. Proteins also serve as messengers for signal transmissions (e.g., hormones thet
help communicate between tissues and organs). They are also known as carriers of atoms and
small molecules within cells. Proteins also aid in the body/s defense as antibodies that bind to
foreign particles like bacteria and viruses.
PROTEIN SOURCES DIFFER
Most so-called complete proteins come from animal sources
Quality Complete® Nonallergenic*
Whey protein isolate 1.00 v x
Casein 1.00 v x
Soy Protein isolate 1.00 ¥ x
Egg white powder 1.00 ¥ x
Beef 0.92 v v
Chicken 092 Vv v
Pea proteinisolate. 0.82 x v
Canned lentils * 052 x v
Hemp seed ost x v
Whole algal protein 0.51 4 v
Wheat gluten 025 x x
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igre 54, Source of proton ia he human detExamples of Protein Functions
Immunoglobulin 6 (gg
Antibody (Ab) Known as immuneglobouling (9),
those are ¥shaped proteins tat help
Born mm Xs) _ | inprotecting the body by fighting al
hid iokign bos coed nigens
Figure 85, Bsc once ofA
Enzyme These are biomolecules that speed | Phenylalanine
up the chemical reaction inthe cals.
These are vital in lfe processes like
digestion and metabolism. They
also assist inthe formation of new
‘molecules by roading the genetic
information stored in the ONA.
hydroxylase
Figure 8.7. Sample activity fa messenger
hormone
Messenger proteins are proteins
that transmit signals to coordinate
biological processes between different
cell, tissues, and organs.
Growth hormone
Structural component
Figure 5.8, cin and myouh taert
‘Those are a type of protein that
provides structure and suppor for cells
Actin,
MyosinTransport/storage These are proteins that bind and Ferritin
carry molecules within the cells and
throughout the body.
Figure 5.9. Transport proteins inthe cel