Can you please explain to me how to approach this problem? it’s confusing to me.
~ | Practice_ midterm + answers . . pdf- 71[13801 . pdf*X+|XV|@ file : / / / C : / Users / 1949 4 / App Data / Local / Packages / microsoft windows communicationsapps_ & wek y b 3 dobbwe / LocalState / Files / 50 / 150 / pdf – 1 1 1 1380 1 . pdf)…4\of 7| 8[ ] Fit to width` A Page viewA " Read aloudUn Add notes|Score ,Bio9& A Midterm 02 / 13 / 12 Name*SIDplease donot write in13 . ( 3 pt ) You have a peptide that has 4 Cys residues with the following sequence*hereGlu – Asp- Ala- Cys- Phe- Ser- Cys- Pro- Gly- Ala-Tyr- Thru Glu- Ala-Arg- Cys- Phe- Cys- ASnYou modify the peptide with jodoacetamide and then do an amino acid analysis and find*that there are 2 free Cys residues . You next denature a fresh sample of the peptide anddigest with chymotrypsin ( recognizes aromatic residues , cleaves at C-terminus ) . A totalof 3 peptides are generated which you isolate by HPLC . YOU then treat each peptide*with DTT ( cleaves disulfide bonds ) and carry out an amino acid analysis on eachpeptide . Unfortunately your analysis is not quantitative and all you get is total*composition for each peptide – see below)Peptide 1Peptide 2Glu , Ala , Phe , Cys , AspAsh , CysPeptide 3Arg , Ala , Cys , Gly , Glu , Ser , Tyr , Thry Phe , ProJero . comarce wasThis peptide contains a disulfide bond , indicate which Cys residues are tied up in an S-Sbond . Draw a line connecting the 2 Cys residues .`Glu – Asp- Ala- Cys- Phe- Ser- Cys- Pro- Gly – Ala – Tyr- Thru Glu- Ala- Arg – Cys – Phe- Cys- ASn*All or nothinghis stuckyd viaI new notification` O Type here to searchPE
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