o-H H. Hy-H H. From the N-terminus, this sequence is found on the 125th residue onwards. Based on this information, is the protein where this fragment is found in a globular protein, or fibrous protein? Justify your answer
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- Upload a drawing of Gly-Met-Asn-Glu-His Label the alpha carbons Label the R groups as hydrophobic or hydrophilic Label the acidic and basic R-groups Label the peptide bonds Label the N terminus and the C terminusQuestion:- 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 accomplishedProtein Structure and Function A common strategy in the regulation of protein function is to alter its structure. Describe two specific strategies used by the cell to alter a protein’s structure, thereby altering its function.
- Leu-Trp-Phe-Met-Ala-Ile-Val- Draw the structure of the peptide at pH7.4. and Indicate the hydrogen bonds formed in the alpha helix.how many amino acids and omega bonds? How many amino acids appear to have undergone a post-translational modification? how many amino acids which would be classified as polar uncharged amino acids?Beta ( ? ) sheets are a type of secondary structure in proteins. A segment of a single chain in an antiparallel ? sheet has a length of 80.5 Å . How many residues are in this segment?
- Reposting - What would the tertiary structure of the dipeptide Asp-Ser be if it was made into a polypeptide chain? (Would it form a beta pleated sheet, an alpha helix, etc) Why would it do this? What properties of this polypeptide causes this? This sub part still needs to be solved - What would the tertiary structure of Pro-ala and Glycl-L-alanine be?Draw out this peptide using condensed or line-bond structures: His-Thy-Phe-Cys-Glu examine your drawing of peptide for each amino acid, indicate what type(s) of interactions it can contribute to protein tertiary structureAla-Arg-Val-His-Asp-Gln Given the polypeptide chain above Estimate the net charge of the polypeptide chain at physiological pH (7.4) and at pH 5.0 . How many peptide bonds are there? What kind of polypeptide is it?
- Hydropathy plot analysis of your protein of interest reveals a single, prominent hydrophobic peak. However, you later discover that this protein is soluble and not membrane associated. Explain how the hydropathy plot may have been misleading.Protein: HemoglobinCircle and underline each codon, amino acid sequence, make a mutation of the 3rd codon in the nucleotide sequence and circle the affected areas, show the amino acid area with the mutation.Lastly, describe the impact on the protein."MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFR"Ala-Phe-Pro-Cys-Clu-Arg-Arg-Pro-His-Gly-Lys-Clu Calculate the net charge on the polypeptide at a. pH 1.5 b. pH 8 c. pH 13