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Amino acids,Peptides,and Proteins - Coggle Diagram

- - - - pKa
      - Buffer
    - - Net charge of zero
      - Least soluble in water
- - - - α helix
      - β sheet
      - collage triple helix
      - β turn
    - - Fibrous
      - Globular
  - - - Crystalline parts(fibroin rich)
      - Rubber-like stretchy parts
  - - - all α helix
      - all β sheet
      - both
  - - - Steps needed
        • purify the protein
        • crystallize the protein
        • collect diffraction data
        • calculate electron density
        • fit known amino acid residues into density
      - pros
        • no size limits
        • well established
      - Cons
        • difficult for membrane proteins
        • cannot resolve (see) hydrogens
    - - Steps needed
        • purify the protein
        • dissolve the protein
        • collect NMR data
        • assign NMR signals
        • calculate the structure
      - pros
        • no need to crystallize the protein
        • can see many hydrogens
      - Cons
        • difficult for insoluble proteins
        • works best with small proteins
- - - - Forces the proline ring into a favorable pucker
      - Offers more hydrogen bonds between the three
        strands of collagen
      - The posttranslational processing is catalyzed by prolyl hydroxylase and requires a-ketoglutarate, molecular oxygen, and ascorbate (vitamin C).