Proteins Biochemistry

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stefanyoli787
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237733
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Proteins Biochemistry
Updated:
2013-09-29 18:54:48
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Proteins Biochemistry
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proteins in biochemistry
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  1. Primary structure (1°)
    amino acid sequence with its polypeptide chain
  2. Secondary structure (2°)
    local spatial arrangement of the polypeptide chain without regard of the structure of the amino acid residues
  3. Tertiary structure (3°)
    three-dimensional structure of a polypeptide chain
  4. Quaternary structure (4°)
    refers to the spatial arrangement of the protein’s subunit
  5. Homologous
    proteins that perform the same function in different organisms
  6. Homologous example
    Hemoglobin transports oxygen in all vertebrates
  7. Homologous proteins are divided in
    • Orthologous
    • Paralogous
  8. Orthologous
    proteins from different species that have homologous a.a. sequences and arose from common ancestral gene
  9. Paralogous
    proteins found within a single species that have homologous a.a. sequences. They arose form gene duplication
  10. Paralogous example
    α and β globulin chains
  11. Allowed Conformations of Polypeptides Are Indicated by the
    Ramachandran Diagram
  12. P (pitch)
    the distance the helix rises along its axis per turn
  13. n
    number of peptide units per helical turns
  14. In β pleated sheets
    hydrogen bonding occurs between neighboring polypeptide chains rather than within one as in α helices
  15. β pleated sheets come in two varieties:
    • Antiparallel pleated sheet
    • Parallel pleated sheet
  16. Antiparallel pleated sheet
    Neighboring hydrogen bonded polypeptide chains run in opposite directions
  17. Parallel pleated sheet
    The hydrogen bonded chains extend in the same direction
  18. A protein’s primary structure dictates
    its three-dimensional structure
  19. Levinthal’s paradox
    Many conformations are possible for a typical protein that the protein does not have sufficient time to reach its most stable conformational state by sampling all the possible conformations.
  20. Molecular Chaperonins
    Proteins that direct the proper folding of proteins due to hydrophobic interactions of side chains that might cause a defect in folding

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