I have an exam on Water and Carbon, Proteins Structure and Function and Nucleic
ID: 8658 • Letter: I
Question
I have an exam on Water and Carbon, Proteins Structure and Function and Nucleic Acids and the RNA World. I understand the chapters to an extent, but I need help with a few things.I'm not exactly sure how you can tell whether or not an R-group on a protein makes it polar or non-polar. I know the amino group and carboxy group will be charged already and they cancel each other out.
I also don't understand what a peptide bond is and what it's function is and the same thing goes for Heat Shock Proteins.
I still am trying to find a broader difference between Competitive Inhibition vs. Allosteric Regulation.
And my very last question is what is a phosphodiester bond in simple terms and what is its function?
help very much appreciated. Thanks
Explanation / Answer
A peptide bond is a bond that forms between two molecules, specifically the amino acids, where the carboxyl group bonds with the amino group. Depending on how many bonds are formed we can either get a dipeptide(2 amino acids linked) or a polypeptide(many linked). For the difference between competitive inhibition vs. allosteric regulation is that competitive inhibition is when a non-reactive compound resembling a certain substrate will bind to the active site of a protein. It does this by "competing" with the subtrate until it binds therefore no substrate can anymore(does not react with enzyme). Allosteric regulation is when a compound binds to the allosteric site of an enzyme and changes the enzyme so no substrate can enter active site. The allosteric substrate is usually a product of the last enzyme in a enzyme chain therefore once too much product is formed it binds to the first enzyme(allosterically) and stops the process. Lastly a phosphodiester bond is the bond between the 3' end of a nitrogous base and the 5' end of another nitrogous base in what is known as the "backbone" of DNA. This is important in keeping the structure of DNA stable and connecting adjacent nitrogous bases. Hopes this helps
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