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The side chain of which of the following amino acids is most hydrophilic
Phe
Val
Leu
Cys
Ala
The hydrophobicity or hydrophilicity of the amino acids in a protein is quantitatively analysed using a hydrophilicity plot. It is used to describe or pinpoint a protein's potential structure or domains.
-The plot's x-axis represents the amino acid sequence of a protein, and the y-axis represents the degree of hydrophobicity and hydrophilicity.
- The degree of interaction between particular amino acids and polar solvents like water can be determined using a variety of techniques. For instance, the Hopp-Woods scale assesses hydrophilic residues while the Kyte-Doolittle scale identifies hydrophobic amino acids.
Hopp-Woods scale - The Hopp-Woods hydrophilicity scale of amino acids is a technique for ordering amino acids in a protein according to their water solubility in order to look for surface locations on proteins, particularly those locations that tend to form strong interactions with other macromolecules like proteins, DNA, and RNA.
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- Which of the following is incorrect about the peptide Arg-Asp-Cys-Tyr-Gln-Arg-Glu? It has six peptide bonds b. It has a net charge of zero at pH 7 It has six charged groups at pH 7 d. None; all the other choices are correct a. C.arrow_forwardWhich of the following describes the most likely outcome of a mutation that causes a sin- gle amino acid to be removed from a protein subunit? A It will affect the primary, secondary, and tertiary structures of the protein. B с D It will affect the secondary and tertiary structures of the protein but not the primary structure. There will be no observable effect on the structure of the protein. It will change the primary structure of the protein without affecting other structures in the protein.arrow_forward
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