1. B Y G R O U P 3
A N N I S A F A D I L A H T R G
D U R R I Y A H L B S
L E T T Y N A I N G G O L A N
P U T R I D I A N H A M I A N
S O H M I Y A T I L I N G G A
Biochemistry:
“PROTEIN”

2. What is Protein??
 Protein is a macro nutrient composed of
monomer form amino acids that is necessary for
the proper growth and function of the human body.
 Amino acids are small molecules that contain
carbon, hydrogen, oxygen, and nitrogen atoms; two
also contain sulfur atoms.

3.  A chain amino acids is called a polypeptide
chain

4. The structure of Amino
acid

5. How can we get Protein?
A set of essential amino acid we obtained from
animal and/or vegetable protein sources.

6. Legumes
 Peanut
A 1-cup serving of raw peanuts contains 828
calories and 38 grams of protein. Peanuts lack the
essential amino acid L-methionine, but contain high
levels of the other essential amino acids, including L-
lysine.

7. Cereal and grains
 Cereal and grains
 Cereal rich of carbohydrates, complete protein, low
fat, and rich of rough fiber.

8. Animal
 Seafood (compelete protein)
A 3.5 ounce salmon filet contains
about 27 grams of protein, while a
single six ounce can of tuna holds a
whopping 40 grams of the body-
building macronutrient.

9. Fruits
 Fruits
Fruits can be a good source of protein, though
they tend to provide less than vegetables, beans, and
legumes. When looking for protein, dried fruits and
berries are best.

10. Vegetables
 Vegetables
Eat more of green vegetables, because
green vegetables contain more protein
than other vegetables. So the protein
needed in our body enough to get.

11. Functions of Protein
Biological function
Structural proteins , has function to
support.
(Microtubule and microfi lament proteins form
supporting fibers inside cells; collagen and other
proteins surround and support animal cells; cell wall
proteins support plant cells.)

12. Enzymatic proteins, Increase the rate of
biological reactions.
e.g
 DNA polymerase increases the rate of duplication
of DNA molecules; RuBP carboxylase/oxygenase
increases the rates of the first synthetic reactions of
photosynthesis; the digestive enzymes lipases and
proteases increase the rate of breakdown of fats
and proteins, respectively.

13.  Membrane Transport proteins, To Speed up
movement of substances across biological
membranes.
E.g :
 Ion transporters move ions such as Na, K, and Ca2
across membranes
 Glucose transporters move glucose into cells
 Aquaporins allow water molecules to move across
membranes.

15.  Motile proteins, to produce cellular
movements.
e.g.:
 Myosin acts on microfilaments to produce muscle
movements
 dynein acts on microtubules to produce the
whipping movements of sperm tails, flagella, and
cilia
 kinesin acts on microtubules of the cytoskeleton

16.  Regulatory proteins, Promote or
inhibit the activity of other cellular
molecules.
e.g.:
 Nuclear regulatory proteins turn genes on or off to
control the activity of DNA.
 Protein kinase add phosphate groups to other
proteins to modify their activity.

18. Receptor proteins, to bind molecules at
cell surface or within cell; some trigger
internal cellular responses.
e.g.:
 Hormone receptors bind hormones at the cell
surface or within cells and trigger cellular
responses.
 LDL receptors bind cholesterol-containing
particles to cell surfaces.

19.  Storage proteins, Hold amino acids and
other substances in stored form.
e.g.:
 Ovalbumin is a storage protein of eggs
 Apolipoproteins hold cholesterol in stored form
for transport hrough the bloodstream.

20.  Venoms and toxins, Interfere with
competing organisms Interfere with
competing organisms.
e.g.:
 Ricin is a castor-bean protein that
stops protein synthesis.
 Bungarotoxin is a snake venom
thatcauses muscle paralysis.

21. Physical funtion
Proteins form the basis of cells, which come
together to form organs, muscle tissue, bones, skin,
hair and nails.
 help organize your cells into separate tissues and
they can protect the body as well.
 for example, specialized proteins tightly connect one
skin cell to another to create a cohesive barrier
against the outside environment.

22. Classification of Protein
 Based on Their needed in our body.
o Essential (very needed, cannot synthesize,
cosume via diet)
o Conditionally essential (not always
needed)
ex: a young and growing individual, or
during illness.
o Non-essential amino acids ( needed, can
synthesize)

23. Essential amino acids:
• Histidine, Isoleucine, Valine , Leucine, Lysine,
Methionine, Phenylalanine, Threonine,
Tryptophan
Non Essential amino acids:
 Alanine, Asparagine, Aspartic acid, and
Glutamic acid.
Conditionally amino acids:
 Arginine, Cysteine, Glutamine, Tyrosine,
Glycine, Ornithine, Proline, and Serine.

24. •Based on the sidegroup

27. Structure of Protein.
 Proteins have four level of structure. each level has
different characteristics and degrees of structural
complexity to the molecule.
 Primary structure is the particular and sequence of amino
acids forming a polypeptide.

28.  secondary structure is produced by the
polypeptide chain twists into coil (helix)
and turns of the amino acid chain.

29. Tertiary structure is the folding of the
amino acid chain into a functional
domain such as a barrel or pocket with its
secondary structures, into the overall
three-dimensional shape of a Protein.
In this example, the coils of a globin chain
form a pocket

30.  Quaternary structure, when present,
refers to the arrangement of polypeptide
chains in a protein that is formed from
more than one chain. Hemoglobin, shown
here, consists of four globin chains ( brown and
blue). Each globin pocket now holds a heme group
(red ).

31. Disease and clinical diagnose caused by protein
 Changes in a protein’s shape may have drastic
consequences to health. And can cause disease.
 If proteins get denature, it will affect to their
function.

32. Disease caused by the changing shape of protein:
 Prion diseases (Prions are misfolded
 proteins), including mad cow disease (bovine
spongiform encephalitis, or BSE) in cattle. Affect the
nervous system
The symptoms:
 hard to diagnose until it has nearly run its
course.
 people have symptoms related to the nervous
system
 depression and loss of coordination
 Dementia develops (the loss of mental functions
such as thinking, memory, and reasoning that is severe
enough to interfere with a person's daily functioning

34.  Creutzfeldt-Jakob disease in humans
 CJD is a degenerative neurological disorder (brain disease)
that is incurable and invariably fatal.
The symptoms:
• leading to memory loss, personality changes and
hallucinations
• physical problems such as speech impairment, jerky
movements (myoclonus), balance and coordination
dysfunction (ataxia), changes in gait, rigid posture, and
seizures.
• CJD can be fatal within months or even weeks

35. How can diagnose?
 Standard diagnostic tests include,
 A spinal tap (rule out common causes of dementia
)
 Electroencephalogram (EEG) to record the brain’s
electrical pattern
 Computerized tomography of the brain ( know the
symptoms caused by another problem like can
stroke or tumor)
 Magnetic resonance imaging (MRI) brain scans
also can reveal characteristic patterns of brain
degeneration that can help diagnose CJD.

37.  Scrapie in sheep,is a fatal, degenerative disease
affecting the central nervous system of sheep and
goats.
 The diseases classified as transmissible spongiform
encephalopathies (TSE).
 The disease apparently causes an itching sensation
in the animals.

38. Clinical sign and diagnosis
The symptoms:
 There may be behavioural changes and maybe an
increase in chewing movements.
 Ataxi.a and neurological signs then develop.
 Some sheep scratch excessively
 show patches of wool loss and lesions on the skin.
 weight loss, anorexia, lethargy and possibly death.