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- Question What is the net charge for the following peptide at pH = 7 (neutral pH)? Ser-Trp-Arg-Gln-Glu-His-Lys-AspPeptide sequence using 1-letter code for amino acids: EDLSMTCFRH What is the net charge of this peptide at pH 9? Use the pKa values from Table 4-1 from Voet, Voet and Pratt. -2 -1 O +1 +2Purification of a new unknown protein that you isolated from tissue and Assume that you have reached the following data during the characterization; Gel filtration: Gel filtration in protein native conformation When chromatographed, it has a molecular weight of 240000 daltons (240 kDa) is detected to be around. Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride subjected to gel filtration chromatography again under denatured conditions. is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa) a protein is obtained. SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol (Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons. Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa) is observed. In the light of these findings, the quaternary/quaternary…
- GABA (B) Need help answering these questions about the GABA(B) protein. What class (globular, fibrous, membrane) protein is the protein Identify the organism (or organisms that have this protein) Identify the cellular location of this protein Describe the function Find the primary structure (list it on a slide) Describe secondary structure (alpha-helix, beta sheet, and how many of each and what percent of the total protein) Find a picture of the tertiary structure (which should also show secondary structure) Does the protein have a quaternary structure, if so what is it?Determining 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?GTTTTCACTGGCGAGCGTCATCTTCCTACT 10. Generate a secondary structure prediction for one identified protein.
- 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?GABA (B) protein Need help answering questions about the GABA(B) protein. What is the primary structure Describe secondary structure (alpha-helix, beta sheet, and how many of each and what percent of the total protein)What is the tertiary structure (which should also show secondary structure)Does the protein have a quaternary structure, if so what is it?PEPTIDE #1: Pro-Phe-Thr-Cys PEPTIDE #2: Gly-Tyr-Ser-Asp Calculate the pI of both peptides. Which is more acidic and why? Which one is more hydrophobic? Which peptide sequence (#1 or #2) would be more likely situated on the surface of the protein?
- Question:- Give a brief description of what the term ‘native protein’ state refers to. Your answer should make a specific reference to how the structural organisation of this state is accomplishedUnderstanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.a 3d structure of protein with acces number of P02008 at uniprot database.