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Home Q & A Board Biology-Related Homework Help Cell Biology
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BRicci BRicci
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9 years ago
Amino acids are commonly grouped as nonpolar or as polar, based on the properties of the side chains.  The properties cannot readily be determined from the free amino acids.  Why are the properties of the side chains difficult to measure using free amino acids?
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#1
9 years ago
It really depends on a method you are using for measuring. It's hard to understand which properties are you trying to figure it out? Please be more specific.
Life isn't about waiting for the storm to pass....it's about learning yo dance in the rain[/size]
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#2
9 years ago
Partitioning methods have many drawbacks. First, it is difficult to mimic the protein interior. In addition, the role of self solvation makes using free amino acids very difficult. Moreover, hydrogen bonds that are lost in the transfer to organic solvents are not reformed but often in the interior of protein.
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#3
9 years ago
Thus, the hydrophobicity/hydrophilicity of a free amino acid is not the same as that of its side chain in a protein. To measure the hydrophobicity/hydrophilicity of the side chains, it is common to assess the properties of side-chain analogs. Thus, for alanine one would use methane, for threonine, ethanol, for aspartic acid, aceticacid, and so on.To assess hydrophilicity, one can
measure the solubility of the side-chain analogs in water.
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