1. Lets start by determining the products we would get from treating a polypeptide with some of the procedures above. Using the polypeptide A-R-D-K-P-C-F-M-P-N-G A) What would acid hydrolysis give you? What would you get if you used Chymotrypsin? B) What would you get if you used Cyanogen bromide? C) What would you get if you used Trypsin? How about using Trypsin after aminoethylation?
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- Confirm Regularly bring your favourites, password... of 45 OCR 2021. You may photocopy this page. 7 of 46 Create 4 Which of the following nucleotides contains uracil? A B NH H,C. ofo HN HO-P-O- HO-P-O- OH ОН ОН OH 'NH HO-P- NH, HO-P-O OH ОН ОН OH Your answer An anticodon seguence of five successsive tRNA molecules involved in protein sunthosie was arDetermining the amino acid sequence in a protein usually in- volves treating the protein with various reagents that break up the protein into smaller fragments that can be individually sequenced. Treating a particular 11-amino acid polypeptide with one reagent produced the fragments: Ala-Leu-Phe-Gly-Asn-Lys Trp-Glu-Cys Gly-Arg Treating the same polypeptide with a different reagent pro- duced the fragments: Glu-Cys Gly-Asn-Lys-Trp Gly-Arg-Ala-Leu-Phe What is the amino acid sequence of the polypeptide?light reaction - Google: Jod. google.com/document/d/1plhyciPrM-AMsQKmaUHZSZU44EJL85jDuCyDxE01E60/edit NLEY-protein-synthesis-worksheet_practice-converted @ w Insert Format Tools Add-ons Help Last edit was 7 minutes ago 100% - Normal text Noto Sans . BIUA 12 川, 三三▼ 3 5 Y 6. 7 I 3. DNA → TAC CTT GGG GAA TAT ACA CGC TGG CTT CGA TGA ATC CGT ACG GTA CTC GCC ATC MRNA → protein → 4. DNA → TAA ACT CGG TAC CTA GCT TAG ATC TAA TTA CCC ATC mRNA → protein → 5. DNA - CTA TTA CGA TAC TAG AGC GAA TAG AAA CTT ATC ATC MRNA → protein → Sign out 围 Ce & 6. 8. 3. de 5
- flow chart of purification steps of Beta-fructofruanosidase (Invertase)topic: Bradford AssayThere are numerous methods of protein determination in use, but this module focuses on the Bradford assay.The Bradford assay is a dye-binding method that employs Coomassie Brilliant Blue G-250, whose structureis shown in Figure 2.3.4.1. Coomassie Brilliant Blue G-250 is a dye that interacts with proteins throughhydrophobic and electrostatic interactions. What are the identities and functions of the components of the Bradford reagent in protein contentdetermination?E. PROTEIN PRIMARY STRUCTURE ELUCIDATION. 1. Determine the primary structure of the protein described below. Write the final sequence using the corresponding three-letter code for each amino acid. Example: M-F-Y-R should be written as Met-Phe-Tyr-Arg Treatment with cyanogen bromide and sequencing yields the following peptide fragments: o D-M o R-A-Y-G-N o L-F-M Chymotrypsin digestion and sequencing yields the following peptide fragments: o G-N D-M-L-F o M-R-A-Y o o
- Given: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?ok-Personal Microsoft Edge com/maildeeplink 021 pdt Download Print Save to OneDrive 1. Draw the structure of the pentapeptide Gln-Trp-His-Glu-Tyr that would predominate in aqueous solution at pH3D10.3. (Relevant pka values are: 2.2 4.3, 6.0, 9.8, and 10.1) Acp is adiusted toAffinity chromatography You have created a fusion protein tagged with Glutathione-S-Transferase (GST). Your lab mate tells you that the affinity columns for this type of tagged protein are very similar to that of Histadine tagged proteins. Using the following elements set up a purification column and construct a protocol for an affinity purification using this tag. A large amount of glutathione is usually used to elute the tagged protein off the column. How might this work?
- Antimicrobial Corning®Gorilla®Glass Protein Synthesis IT Uonsan Review Base your answer to the question on the diagram below, which represents a process that occurs in living cells, and on your knowledge of biology. Newly formed molecule Glycine Arginine Proline HAlanine Glycine CỦA MRNA Structure X The process shown in the diagram is 1. cellular respiration 2. cellular reorganization 3. gene recombination 4. protein synthesis Zoom: Standard EX Note Bookmark Eliminator Highlighter P Line Reader Calculator Ruler Reference Protractor Coming soonPart C - Exploring antiparallel 3 sheet structure The hydrogen bonding between antiparallel sheets, also visible in the pdb by selecting the antiparallel sheet view, is shown. Locate the N- and C-termini in this image. Select the antiparallel sheet view in the pdb file. How many peptide chains are shown? O 1 O 2 3 O 4 Submit Request Answerdisadvantage of using protein blast