BE201 Lecture 3 Primary Structure

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Across
  1. 4. In gel filtration, the [Blank] molecules emerge last
  2. 7. Chromatographic separation on the basis of binding specificity
  3. 9. One of the enzymes used to cut up peptides for mapping
  4. 10. Chromatographic separation on the basis of size
  5. 13. Physical process used to break up a tissue to create a crude protein mixture
  6. 14. A type of mass spectrometry used for sequencing proteins
  7. 16. Chromatographic separation on the basis of charge
  8. 19. A reagent that cuts peptides after methionine residues
  9. 21. PITC is another name for [Blank] reagent
  10. 22. Where Edman Sequencing commences in a protein
Down
  1. 1. Physical process used to change the buffer in a protein mixture
  2. 2. The graphical readout from a HPLC
  3. 3. An evolutionarily conserved portion of a protein
  4. 5. A reagent that cuts peptides after F residues
  5. 6. Protein sequencing enables comparisons between normal and [Blank] proteins
  6. 8. A property used to separate proteins
  7. 11. Amino acid represented by the letter K
  8. 12. Metal exploited during His-Tag chromatography
  9. 13. Peptide sequencing works best on [Blank] peptides
  10. 15. Solution used to elute protein from an ion-exchange column
  11. 17. Units/Mg on a purification table
  12. 18. Physical process used to turn crude protein into semi-pure fractions
  13. 20. A chemical method used to break down proteins into amino acids