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Flashcards

Protein Structure and Fuction

Natalie Caughlin Biology Undergraduate English 54 cards

What are the four main sections/parts of an amino acid?

Cards in this deck (54)

  1. 1True of False: Not all proteins are enzymes, but all enzymes are proteins.True. Not all proteins are enzymes, but all enzymes are proteins.
  2. 2What are antibodies?Proteins that act as flags and mark cells or invaders for destruction.
  3. 3What are the four main sections/parts of an amino acid?A central carbon, an amino group, a hydrogen, a carboxyl group, and a side chain or R group.What are the four main sections/parts of an amino acid?
  4. 4What do R groups do to amino acids?They make each amino acid unique and contain chemical and physical properties that allow the amino acids to be grouped.
  5. 5What are the three ways to group amino acids based on their properties?hydrophobic and hydrophilic
    polar and nonpolar
    basic and acidic
  6. 6Why are an amino acid's properties so important?They influence the way that the protein folds.
  7. 7What relationship does a protein have with its shape?The shape of a protein equals its function.
  8. 8Where are hydrophobic amino acids found?Found in the interior of a protein.
  9. 9How are hydrophobic amino acids stabilized/ bonded?Van der Waals/ London dispersion forces create temporary changes causing the amino acids to be attracted to each other
  10. 10What are the three categories of Hydrophilic amino acids?Polar, basic, and acidic
  11. 11How are basic and acidic amino acids differentiated?By charge. Basic have a positive charge, and acidic have a negative charge.
  12. 12Do basic and acidic hydrophilic amino acids interact?Yes. They can bond together through ionic bonding
  13. 13Where are hydrophilic amino acids located in a protein?They are folded to located on the outside of the protein.
  14. 14What are the three special amino acids?Glycine, proline, and cytosine.
  15. 15Which special amino acid creates a disulfide bond?Cytosine
  16. 16What is Glycine's R group, and what effect does it have?Single hydrogen. This makes the amino acid symmetrical, allowing atoms to rotate more freely and increasing the flexibility of the protein backbone.
  17. 17What is proline's R group, and how does it effect the protein?A ring structure that kinks and puts a strain on the nearby amino acids.
  18. 18What is cytosine's R group, and how does it effect the protein?An SH, or thiol group, which can attach to other cytosines in the same or different proteins, creating a disulfide bond.
  19. 19What does a peptide bond connect?Connects an amino acid group to a carboxyl group.
  20. 20What does the "backbone" include in a polypeptide?Everything but the R groups in connected amino acids. I.e. carboxyl group, H, alpha carbon, amino acid group
  21. 21True or False: Can R groups extend past the backbone in a polypeptide?True. R side chains extend past the backbone and interact with one another
  22. 22What is a three letter sequence representing an amino acid called?A codon
  23. 23What can a codon be simplified to?Can be simplified to a one-letter abbreviation for the corresponding amino acid that it represents
  24. 24What are the four stages of structures in a protein?Primary, secondary, tertiary, and quaternary
  25. 25What is the primary structure of a protein?The amino acid sequence. Read in order and determines every other layer of structure.
  26. 26How is the amino acid sequence read in the primary structure?Read from the amino acid end toward the carboxyl end.
  27. 27Describe the Secondary Structure in proteins.The result of Hydrogen bonding in functional groups of the backbone. Alpha helix and beta sheet are created.
  28. 28What is the alpha helix?A tightly coiled polypeptide chain
  29. 29What is a beta sheet?A pleated sheet caused by the polypeptides folding back and forth on itself
  30. 30True of False: Polypeptide chains in a beta sheet can only be run antiparallelFalse. Beta sheet polypeptides can be run parallel or antiparallel.
  31. 31Describe the Tertiary protein structure.3D, global folding of, usually several, secondary structures determined by the R groups (polar, hydrophobic, hydrophilic, etc.)
  32. 32Describe the Quaternary structure of a protein.When two polypeptides bond and form a single protein. Assembly of multiple tertiary structures.
  33. 33How is a disulfide bond formed?Formed by oxidation reaction of thiol groups from two cysteines either within the same protein or between two different proteins.
  34. 34How is a disulfide bond broken?A reduction reaction breaks breaks the disulfide bonds and reforms the thiol groups
  35. 35Define Domain.A segment of polypeptide that can fold into a compact stable structure.
  36. 36What are domains known for?Known for taking a particular shape and performing a particular action.
  37. 37Another way to describe a protein's shape.Protein confirmation
  38. 38What is the loss of biological activity of a protein called?Denaturation.
  39. 39What happens during denaturation?Due to various agents like incr. temp., pH, ionic strength, or solubility a protein unfolds and loses its function.
  40. 40What is the process that restores a protein's function after denaturation?Renaturation.
  41. 41What happens during renaturation?Protein function is restored by restoring pH, lowering temperature, etc., causing the protein to refold.
  42. 42What happens when proteins do not fold together correctly?Many diseases are the result of protein misfolding, especially an accumulation of misfolded proteins.
  43. 43What is a prion?An infectious, misshaped protein. These can encourage other proteins to misfold, which can lead to disease progression.
  44. 44What are the four ways that cells can regulate proteins?Gene expression
    Compartmentalization
    Interaction with other molecules
    At the protein level itself
  45. 45What is feedback inhibition?A common type of control when a molecule other than a substrate binds to a protein at a regulatory site rather than an enzyme's active site to halt production.
  46. 46What is it called when a pathway is inhibited by build up of a product?Negative Feedback
  47. 47Describe multiple feedback inhibition.There are multiple pathways and reactions interacting at once. Products can inhibit production at different points, which may or may not effect other reactions taking place.
  48. 48What is a catalytic site on a protein? What happens at this site?A site where a substrate bonds. This substrate is then converted into a product before it is released, leaving the protein open for another substrate.
  49. 49What is an allosteric site on a protein? What happens at this site?A site where a regulatory molecule bonds. This causes conformational change
  50. 50True or False: Very few proteins are allosteric proteins, meaning they have allosteric sites allowing for protein regulation.False. Most proteins are allosteric proteins.
  51. 51Describe Protein Phosphorylation.An enzyme, kinase, uses the energy of ATP and transfers a phosphate group onto the protein, causing conformational change.
  52. 52What is phosphatase, and how does it relate to protein phosphorylation?An enzyme that catalyzes the removal of a phosphate group, causing dephosphorylation.
  53. 53What is GTP?An energy source like ATP, but with guanine instead of adenosine.
  54. 54Describe GTP-binding protein regulation.GTP is used as energy (on). A phosphate group slowly dissociates and breaks off (inactive). GDP then falls from the protein, and another GTP is quickly added (on). This cycle continues.

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Undergraduate Biology Flashcards on Protein Structure and Fuction, created by Natalie Caughlin on 25/10/2025.
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