Relatively hydrophobic proteins will require higher amounts of (NH4)2SO4 to precipitate.
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- Mad cow disease is an infectious disease where one misfolded protein causes all other copies of the protein to being misfolding. This is an example of a disease impacting structure. primary secondary tertiary quaternaryif the tetrapeptide shown in the binding site above (Gly-Ser-His-lle) were in an aqueous solution at pH=6.2, what fraction of peptide molecules would have a +1 charge?Despite being hydrophobic, why is methionine (Met) not located within a protein?
- Why is methionine (Met) not found on the inside of a protein even though it is hydrophobic?a peptide has the sequence: Asp-His-Tyr-Asn. What is the net charge on this molecule at pH 7.2?a peptide has the sequence: Asp-His-Tyr-Cys. What is the net charge on this molecule at pH 7.0? Will it have the same net charge at pH 12?
- Globular proteins are typically constructed from several layers of secondary structure, with a hydrophobic core and a hydrophilic surface. Is this true for a fibrous protein such as keratin?draw the peptide structure n-GYSEDAK-c in low pHIn N-linked glycoproteins, the sugar is usually attached to the protein by a bond to the N atom in a side-chain amide. Which amino acids can form such a bond?
- The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.A protein with a quaternary structure is a multidomain protein. Is this always correct? Explain.Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU
