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.© BrainMass Inc. brainmass.com October 24, 2018, 6:55 pm ad1c9bdddf
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 ...
Amino acids and protein structures are embedded.
Type II and Type I Restriction Endonucleases
Please help me answer these questions about restriction enzymes.
What is a restriction endonuclease?
Why do molecular biologists use restriction enzymes?
What is the difference between type I and type II restriction endonucleases and why are type II restriction endonucleases more useful for molecular biologists than type I restriction endonucleases?