CHEM214- Final Exam Guide - Comprehensive Notes for the exam ( 27 pages long!)

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cyanchimpanzee651

29 Mar 2018

School

University of Delaware

Department

Chemistry and Biochemistry

Course

CHEM214

Professor

Hoober

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Document Summary

Characteristics: aspartic acid (proton on) and aspartate (proton off, glutamic acid (proton on) and aspartic acid (proton off, have measurable pka"s, only donate proton at high ph, negative at physiological ph, polar. Amino acids: aspartate (asp, polar, glutamate (glu, polar. Characteristics: have an amid group, are not ionizable, polar. Amino acids: asparagine (asn, polar, glutamine (gln, polar. Proteins: protein fold is based off of its hydrophobicity. Synthetic protein: the more carbons, the more hydrophob ic. We need to know: names of amino acids, amino acid abbreviations, what kind of r group each amino acid has, structures of the 6 amino acids, pka"s of n and c terminus, carboxylic acid, amine. Amino acids pt 2: ionization states of amino acids. Charge on a protein steps: draw all protons on, evaluate at ph given, add all charges. Peptides 1-degree structure determination: determining primary sequence because it dictates functionality, family of protein trees have similar sequences.

Related Questions

1. A polypeptide chain has a large percentage of acidic and basic amino acids in it. The R groups of these amino acids form ionic interactions, which helps the protein to maintain itâs structure. This particular polypeptide works well under an optimum pH of 7. Ignoring effects of strong acids and bases on peptide bonds, what will happen to the tertiary structure of the protein if you move it stomach acid, which has a pH of 1-2. Why? Be specific regarding what influence the pH will have on the bonds maintaining tertiary structure in the molecule. Include the amino acid charges of the acidic and basic amino acids at the acidic pH, as well as the concept of pK in your answer. Assume that acidic amino acids have a pK of approximately 4.7 and basic amino acids have a pK of approximately 10.

2. Ignoring peptide length (or lack thereof) where would this portion of a polypeptide be most likely to be found: On the inside or on the outside surface of a protein floating around in the cytoplasm? Explain

3. A mutation occurs in the SRC kinase such that the tyrosine on the loop over the active site is changed to aspartic acid. This mutation mimics phosphorylation.
a. knowing what you know about the properties of phosphate groups and aspartic acid, why does aspartic acid mimic phosphorylation?
b. What would be the implication of this mutation on the function of the SRC kinase?

CHEM214- Final Exam Guide - Comprehensive Notes for the exam ( 27 pages long!)

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