BALINO OCTOBER 8, 2021 REPORTING

BERIZO 8:00-12:00AM PRESENTATION

PROTEIN
STRUCTURE, FUNCTION AND ASSOCIATED DISEASES

Ma. Teresa Solijon

ILOILO DOCTOR'S COLLEGE MC - BIOCHEMISTRY

 Proteins are the most versatile
macromolecules in living systems and
serve crucial functions in essentially
all biological processes.

WHAT IS PROTEIN?
They do most of the work in cells and
are required for the structure,
function, and regulation of the body’s
tissues and organs.
Protein comes from the Greek word
proteios, meaning "primary" or
"holding the first place." A Dutch
chemist Gerard Johann Mulder,
coined the word protein in 1838.
 PROTEIN
The building blocks of proteins are amino acids, which are small organic

STRUCTURE
molecules that consist of an alpha (central) carbon atom linked to an amino
group, a carboxyl group, a hydrogen atom, and a variable component called a
side chain.
 PROTEIN
STRUCTURE
Proteins are built
from a set of only
twenty amino acids,
each of which has a
unique side chain.
The side chains of
amino acids have
different chemistries.
 PROTEIN
The chemistry of amino acid side chains is critical to protein structure because

STRUCTURE
these side chains can bond with one another to hold a length of protein in a
certain shape or conformation.
Charged amino acid side chains can form ionic bonds, and polar
amino acids are capable of forming hydrogen bonds.
Hydrophobic side chains interact with each other via weak van der
Waals interactions.
The vast majority of bonds formed by these side chains are non-
covalent.
Cysteines are the only amino acids capable of forming covalent
bonds, which they do with their particular side chains.
FOUR LEVELS OF PROTEIN
PRIMARY
STRUCTURE STRUCTURE
SECONDARY
STRUCTURE
TERTIARY
STRUCTURE
QUARTENARY
STRUCTURE
PRIMARY STRUCTURE
The primary structure is the sequence of amino acids that make up a
polypeptide chain. 20 different amino acids are found in proteins. The exact
order of the amino acids in a specific protein is the primary sequence for
that protein.
The next level of protein SECONDARY STRUCTURE
structure, secondary structure,
refers to local folded structures
that form within a polypeptide
due to interactions between
atoms of the backbone. The
most common types of
secondary structures are the α
helix and the β pleated sheet.
Both structures are held in
shape by hydrogen bonds,
which form between the
ALPHA HELIX

In an α helix, the carbonyl

(C=O) of one amino acid
is hydrogen bonded to
the amino H (N-H) of an
amino acid that is four
down the chain.
 BETA PLEATED SHEET
In a β pleated sheet, two or more segments of a
polypeptide chain line up next to each other,
forming a sheet-like structure held together by
hydrogen bonds. The strands of a β pleated
sheet may be parallel, pointing in the same
direction (meaning that their N- and C-termini
match up), or antiparallel, pointing in opposite
directions (meaning that the N-terminus of one
strand is positioned next to the C-terminus of
the other).
TERTIARY STRUCTURE
The overall three-dimensional
structure of a polypeptide is called
its tertiary structure. The tertiary
structure is primarily due to
interactions between the R groups
of the amino acids that make up
the protein. R group interactions
that contribute to tertiary structure
include hydrogen bonding, ionic
bonding, dipole-dipole interactions,
and London dispersion forces-
basically the whole gamut of non-
QUARTENARY STRUCTURE
Many proteins are formed
from more than one
polypeptide chain. The
quaternary structure
describes the way in which
the different subunits are
packed together to form
the overall structure of the
protein.
 Protein
Different visual representation of proteins can give us clues
Representation
about proteins' structure and function
• for space-filling diagram it show all the atoms that makes
up the protein
• for ribbon diagram or cartoon diagram, it shows the
backbone and it highlights the alpha helices.
• for surface diagram, it show the area that are water
FUNCTION OF PROTEIN
 ANTIBODY

Antibodies bind to
specific foreign
particles, such as
viruses and bacteria,
to help protect the
body.
 ENZYME

Enzymes carry out almost all

of the thousands of chemical
reactions that take place in
cells. They also assist with
the formation of new
molecules by reading the
genetic information stored in
DNA.
 MESSENGER

Messenger proteins,
such as some types of
hormones, transmit
signals to coordinate
biological processes
between different cells,
tissues, and organs.
 STRUCTURAL COMPONENT

These proteins provide

structure and support
for cells. On a larger
scale, they also allow
the body to move.
 TRANSPORT/STO
RAGE

These proteins bind and

carry atoms and small
molecules within cells
and throughout the
body.
NUTRITION
SOURCE
Protein is made from twenty-plus basic building blocks called amino acids.
Because we don’t store amino acids, our bodies make them in two different ways:
either from scratch, or by modifying others. Nine amino acids—histidine,
isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and
valine—known as the essential amino acids, must come from food.
The National Academy of Medicine recommends that adults get a
minimum of 0.8 grams of protein for every kilogram of body weight
per day, or just over 7 grams for every 20 pounds of body weight.
Lean meat, fish, eggs, milk and cheese are important sources of
animal protein. All plants contain some protein, but beans, nuts or
cereals are the best plant sources.
ASSOCIATED
DISEASES
KWASHIORKOR
• The deficiency of protein results in the disease kwashiorkor, which is
typically seen in countries where starvation is a problem.
• One of the symptoms of kwashiorkor is a swollen stomach, which ironically makes a child look well fed at first glance.

• The primary symptoms of Kwashiorkor include not only swelling, but

also diarrhea, fatigue, peeling skin, and irritability. Severe protein
deficiency in addition to other micronutrient deficiencies, such as folate
(vitamin B9), iodine, iron, and vitamin C all contribute to the many
health manifestations of this syndrome.
 MARASMUS
• Marasmus is inadequate energy intake in all forms, including
protein.
• Marasmus affects mostly children below the age of one in poor
countries. Body weights of children with Marasmus may be up to
80 percent less than that of a normal child of the same age.
• It is characterized by an extreme emaciated appearance, poor
skin health, and growth retardation. The symptoms are acute
fatigue, hunger, and diarrhea.
 PROTEIN MISFOLDING
ASSOCIATED DISEASES
Protein misfolding is believed to be the primary cause
of
• Alzheimer's disease
• Parkinson's disease
• Huntington's disease
• Creutzfeldt-Jakob disease
• cystic fibrosis
 REFERENCES/SOURCES
• https://www.brainfacts.org/archives/2013/disease -causing-proteins
• https://www.ncbi.nlm.nih.gov/books/NBK21177/
• http://web.fscj.edu/David.Byres/proteins.htm
• https://www.hsph.harvard.edu/nutritionsource/what -should -you -eat/protein/
• https://www.khanacademy.org/science/biology/macromolecules/proteins -and -amino -
acids/a/introduction -to -proteins -and -amino -acids
• http://www.biology.arizona.edu/biochemistry/problem_sets/large_molecules/03t.html
• https://www.mun.ca/biology/scarr/iGen3_06 -04.html
• https://medlineplus.gov/genetics/understanding/howgeneswork/protein/