- There is another melanocyte-stimulating hormone called B-melanotropin. Cleavage of B-melanotropin with trypsin produces the following peptides plus free aspartic acid. WGSPPK DSGPYK MEHFR If you assume maximum sequence similarity between a-melanotropin and B-melanotropin, then what must the sequence of the latter be?
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- There is another melanocyte-stimulating hormone called β-melanotropin.Cleavage of β-melanotropin with trypsin produces the following peptidesplus free aspartic acid. WGSPPK DSGPYK MEHFRIf you assume maximum sequence similarity between α-melanotropin andβ-melanotropin, then what must the sequence of the latter be?Given the R-groups in the peptide GLY-ASN-THR-LYS-HIS. It would most likely be: a)neither soluble nor insoluble because of the need to know the IpH of the peptide b)very water soluble because of it will easily dissolve in water c)easily associating with the water environment because it can H-bond and form dipole-dipole interactions with water d)insoluble in water because the rest of the carbon content of the peptide will not interact with waterApamine is a small protein toxin present in the venom of the honeybee. Ithas the sequenceCNCKAPETALCARRCQQH(a) If apamine does not react with iodoacetate (see Tools of Biochemistry5B), then how many disulfide bonds are present?(b) If trypsin cleavage gave two peptides, then where is(are) the S¬Sbond(s)?
- Draw the molecular formula of the covalently modifi ed histone side chain of acetyllysine. How does this modifi cation alter the chemical properties of the side chain?Calculate the pI for the following tri-peptide: Glu-Arg-LysWhat are the sequences of all the possibletripeptides that contain the amino acids aspartic acid, leucine, andphenylalanine? Use the three-letter abbreviations to express youranswer.
- Replacements such as Lysine -- Arginine and Leucine -- Isoleucine usually have very little effect on protein structure and function.Sars-CoV-2 spike protein: VGIYLQKTSDHRPEFALAMN What is its isoelectric point of this peptide?Draw Glu-His-Trp-Ser-Gly-Leu-Arg-Pro-Gly peptide. What is the net charge of this peptide at pH 3, 8 and 11? What can you say about pI value of this peptide?
- A particular protein has the amino acid sequenceN . . . Ala-Pro-His-Trp-Arg-Lys-Gly-Val-Thr . . . Cwithin its primary structure. A geneticist studyingmutations affecting this protein discovered that several of the mutants produced shortened protein molecules that terminated within this region. In one ofthem, the His became the terminal amino acid.a. What DNA single-base change(s) would cause theprotein to terminate at the His residue?b. What other potential sites do you see in the DNAsequence encoding this protein where mutation ofa single base pair would cause premature termination of translation?Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show them in zig-zag style, from amino to carboxy terminus, with correct stereochemistry Draw the predominant form at pH = 2 Draw the predominant form at pH = 5 Draw the predominant form at pH = 7 Draw the predominant form at pH = 12A recent genome sequencing project for the bacterium Burkholderia mallei has identified a new protein with high similarity to the lysylphosphatidylglycerol flippase enzyme. A short section of the new protein sequence is shown below. TVEVNAPGDVQKALSELQQINDGRLDIRI (a) Are any reverse turns likely to be present? Explain your answer. (b) Are any beta-strands likely to be present? Explain your answer. (c) Are any alpha helices likely to be present? Explain your answer. (d) Is any supersecondary structure likely to be present? Explain your answer. (e) Identify two residues that are likely to be buried in the core of the folded protein. Explain your answer. (f) Identify two residues that are likely to be hydrogen bonded to each other. Explain your answer.