Seal of Good Local Governance (SGLG) 2024Final.pptx
Biochemistry(protein)
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
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.
14.
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.
17.
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)
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
33.
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.
36.
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.