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  1. 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. 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. 3.  A chain amino acids is called a polypeptide chain
  4. 4. The structure of Amino acid
  5. 5. How can we get Protein? A set of essential amino acid we obtained from animal and/or vegetable protein sources.
  6. 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. 7. Cereal and grains  Cereal and grains  Cereal rich of carbohydrates, complete protein, low fat, and rich of rough fiber.
  8. 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. 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. 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. 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. 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. 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. 14.  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
  15. 15.  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.
  16. 16. 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.
  17. 17.  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.
  18. 18.  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.
  19. 19. 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.
  20. 20. 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)
  21. 21. 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.
  22. 22. •Based on the sidegroup
  23. 23. 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.
  24. 24.  secondary structure is produced by the polypeptide chain twists into coil (helix) and turns of the amino acid chain.
  25. 25. 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
  26. 26.  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 ).
  27. 27. 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.
  28. 28. 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
  29. 29.  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
  30. 30. 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.
  31. 31.  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.
  32. 32. 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.