A reverse phase column chromatography separates proteins according to their polarity.  Which pentapeptide will be eluted FIRST when chromatographed at pH 7 using a reverse phase column such as a C-18 column? Peptide Sequence (from N-terminal to C-terminal) AKGED GAAVF ALLLI MCYAG       GAAVF   MCYAG   ALLLI   AKGED

A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the native protein has a molecular weight of 300,000. Chromatography of the protein in the presence of 6 M guanidine hydrochloride (a denaturant) yields a single peak corresponding to a molecular weight of 50,000. Chromatography of the protein in the presence of 6 M guanidine hydrochloride and 10 mM beta-mercaptoethanol (a disulfide bond reductant) yields peaks corresponding to molecular weights of 30,000 and 20,000. What does this data tell you about the structure of this protein? (Be thorough in your answer!)

One of the members of your research group attempted to isolate theenzyme using the protocol you presented. To confirm whether theygot the protein, SDS-PAGE was performed and the gel on the rightwas obtained. Perform the necessary calculations to determine themolecular weight of the suspected band on the gel in the lanelabeled “dialyzed.”

A protein was purified and then analyzed on a size exclusion column. It's molecular weight was determined to be 40,000 Dalton. The SDS-PAGE gel shows one band, corresponding to a molecular weight og 10,000 Dalton. Describe the native conformation of this protein in terms of the number of subunits present and the molecular weight of the subunits.

A At pH 5, what is the net charge of the peptide Val-His-Gln-Cys-Ser-Lys? 0 -1 0 0+1 Ⓒ +2 Q Search "de 96 5 ******* ******* 131183 J- C 8 a hp

On an SDS-gel, If the distance traveled by the bromophenol blue dye is 7 cm, and the distance traveled by the protein band is 2.8 cm, the mobility of the protein is      40     4     40%     0.4

A nonapeptide was treated with dithiothreitol to reduce any disulfide bridges, then partially hydrolyzed, giving rise to the following fragments. What was the sequence of the original polypeptide? Phe-Gln-Asn Pro-Arg-Gly-NH2 Cys-Tyr-Phe Asn-Cys-Pro-Arg Tyr-Phe-Gln-Asn O Cys-Tyr-Phe-GIn-Asn-Cys-Pro-Arg-Gly-NH2 O H2N-Gly-Arg-Pro-Cys-Asn-Gln-Phe-Tyr-Cys O Gly-Arg-Pro-Cys-Tyr-Phe-Gln-Asn-Cys-NH2 Cys-Pro-Arg-Gly-NH2-Cys-Tyr-Phe-Gln-Asn O None of these are correct.

Please provide a separation solution of combining two types of chromatography to isolate the protein A from the mixture containing protein A, B, C and D (shown as below). And then explain the related mechanisms in details. Protein A: Met-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu- Protein B: Met-Asp-Glu-Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu Protein C: Met-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu-Val-Val-Val- Ile-lle-lle-Leu-Leu- Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle- lle-Leu-Leu-Leu-Leu-Val-Val-Val-Ile- Protein D: Met-Asp-Glu--Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu-Glu-Asp- Glu-Asp-Glu-Glu-Asp-Asp-Glu-Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu-Glu- Asp-Glu-Asp-Glu-Glu-Asp-Glu-Glu-Asp

Given the Ramachandran Plot below, identify the protein components that could adopt the phi-psi angle combination indicated by the number 3. (IF YOU COPY UR ANSWER FROM ANOTHER WEBSITE I WILL DISLIKE)

You are analyzing the peptide ala-ile-glu-lys-phe-val- tyr-cys. If you treat the peptide with chymotrypsin, which technique would be best to separate the fragments? O a. ultracentrifugation O b. affinity chromatography O c. dialysis d. gel filtration chromatography O e. ion exchange chromatography What is an advantage of NMR spectroscopy over x-ray crystallography in studying protein structure?