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BIOCHEM: PROTEINS

Karl Olarte Inglés 47 fichas

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  1. 1Structure of proteins: Primary StructureAmino Acid Sequence
  2. 2Structure of proteins: Secondary StructureAmino Acid Interaction
  3. 3Structure of proteins: Tertiary StructureComplex Folding
  4. 4Structure of proteins: Quaternary StructureProtein Complexes
  5. 5Food group that is considered as complete source of proteinMilk
  6. 6Examples of secondary Structures of proteinBeta pleated sheet
    Alpha helix
    Random coil
  7. 7Proteins are long chains of ........?Enzymes
  8. 8Albumins and Globulins are example of.......????Globular Proteins
  9. 9Proteins that mainly function as structural component in living organismsFibrous Protein
  10. 10Process which proteins losses its three-dimensional confirmation caused by proteins unfoldingDenaturation
  11. 11Examples of Fibrous ProteinCollagen
    Keratin
    Elastin
  12. 12play a special role in the structures of many proteins by forming covalent links.Disulfide Bond
  13. 13Chief structural constituents of hair, nails, horns, feathers and hoovesKeratin
  14. 14Homoproteins are example of Globular Proteins that is essential in delivering oxygen throughout the body. True or false?True
  15. 15Amino acids required in human diet that is not synthesized by the bodyEssential Amino Acids
  16. 16How many Amino acids are considered essential?11
  17. 17All amino acids are chiral molecules except.....????Glycine
  18. 18Quantity of amino acids that occurs in proteins20
  19. 19"The arrangements of two or more polypeptide subunits into a single functional complex" Defines what?Quaternary Structure
  20. 20Quantity of amino acids that occurs in nature300
  21. 21a chiral molecule that has left-and right-handed isomersEnantiomers
  22. 22The “building blocks” from which proteins are madeAmino acids
  23. 23Four Groups of Amino AcidsAmino Groop
    COOH (Carboxylic) Group
    Hydrogen Atom
    Side Chains
  24. 24Molecule has an atom bonded to four different groupsChiral molecule
  25. 25two enantiomers of each amino acids are designated by D,L systemD-Dextrorotation
    L-Levorotation
  26. 262 functionalities of amino acidsAcidic Functionality (Acid)
    Basic Functionality (Base)
  27. 27Hydrophobic classification of amino acidsAliphatic Side Chains
  28. 28Heterocyclic/Aromatic is an amino acids which is neither hydrophobic or hydrophilic true or false?true
  29. 29Isoleic point (pI) the pH at which the majority of protein molecules in solution have no net charge True or False?False
    Correction: Amino Acid molecules, not Protein
  30. 30Negatively charged R groupsAspartate
    Glutamate
  31. 31In 1902, he proposed that proteins are long chains of amino acids joined by peptide bondsEmil Fischer
  32. 32Required by infants and growing childrenSemi-Essential Amino Acids
  33. 33the special name given to the amide bond between the a-carboxyl group of one amino acid and the a-amino group of anotherPeptide Bond
  34. 34a molecule containing two amino acids joined by a peptide bondDipeptide
  35. 35a molecule containing three amino acids joined by a peptide bondTripeptide
  36. 36a macromolecule containing many amino acids joined by a peptide bondPolypeptide
  37. 37Protein is a biological macromolecule of molecular weight 5000 g/mol or greater, consisting of one or more polypeptide chainsTrue
  38. 38important in biological oxidation-reduction reactions, has reduced and oxidized form. - It's the most important molecule you need to stay healthy and prevent disease.Glutathione
  39. 39The only other type of covalent bond between aminoacids in proteins and peptides between two cysteine unitsDisulfide Linkage
  40. 40A peptide neurotoxin isolated from the venom of the fish- hunting cone snail Conusgeographicus. - It is a paralytic toxin that blocks nicotinic cholinoreceptors.Conotoxin GI
  41. 41Composed of only amino acids.Simple Protein
  42. 42Fibrous Protein contain permanently associated chemical groups (called as prosthetic groups) in addition toamino acids. true or false?False
    Correction: Conjugated Protein not Fibrous
  43. 43can exhibit a wide range of characteristics, from loss of solubility to communal aggregation.Denatured Protein
  44. 44proteins that contain heme (iron-porphyrin) as a tightly bound prosthetic group . - In myoglobin and hemoglobin, the heme group serves to bind and deliver oxygen.Hemeproteins
  45. 45is found exclusively in red blood cells. >Function: transport oxygen from the lungs to the capillaries of the tissues. - It is the heme group that gives blood their distinct red colorHemoglobin
  46. 46is the most abundant protein in mammals. >It is a major component of tendons, the extracellular matrix of the connective tissues (skin, bone matrix), and the cornea of the eye.Collagen
  47. 47present in walls of large blood vessels (such as aorta). It is very important in lungs,elastic ligaments, skin, cartilage - It is elastic fiber that can be stretched to several times its normal length.Elastin

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Fichas sobre BIOCHEM: PROTEINS, creado por Karl Olarte el 15/11/2022.
Creado por
Karl Olarte · nov 2022
Actualizado
15 nov 2022
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