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    Restriction endonucleases

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    There are four questions to be answered:

    1. What type of amino acid side chains would you expect to find folded on the interior of a globular protein? What kind of experimental evidence supports this claim?

    2. Which amino acid lacks a stereoisomer and which has more than one asymmetric carbon?

    3. What property of the DNA double helix allows us to say that the recognition site for a restriction endonuclease like BamHI (GGATCC) is a structural palindrom?

    4. What general kind of quarternary structure do we expect to find for the restriction endonuclease PstI, which also recognizes a palindromic sructure?

    Research is also given.

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    https://brainmass.com/biology/cell-and-molecular-biology/restriction-endonucleases-52516

    Solution Preview

    Hello

    1) Globular proteins have a tertiary structure that is compactly folded and coiled.

    First, to backtrack: Primary structure refers to the amino acid sequence, which completely determines all other structural features of a protein. This is due to the distinct chemical properties of the amino acid side chains - details which I will leave for your text. each type of protein has particular secondary structural elements; in globular proteins this is mostly alpha-helices. The amino acid residues found in alpha helices are alanine, aspartic acid, glutamic acid, isoleucine, and leucine. In the interior of a ...

    Solution Summary

    Amino acids and protein structures are embedded.

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