CHEM 271 Study Guide - Midterm Guide: Suicide Inhibition, Glutamine, Asparagine

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crimsonyak325

9 Dec 2015

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Document Summary

Slide 13 or 14, lecture 1: has a positively charged side chain at physiological ph. Slide 15, lecture 1 + slide 13, lecture 2: can form disulfide bonds. Slide 14, lecture 1 + slide 21, lecture 3: can form -cation interactions with metal ions. Phe, f or tyr, y or trp, w, structure. (his, Slide 13, lecture 1 + slide 9, lecture 4: acts as a proton shuttle. *slide 18, lecture 8 + (lecture or pg. 269, textbook): (6 points) below is a ribbon drawing of a protein. (1+2+3, clearly identify one region that corresponds to: -sheet; -helix. Slide 14, lecture 4; slide 6, lecture 4. 1: estimate the longest dimension of the -helix that you labeled. Briefly explain how you arrived at your answer. 3. 5 turns * 5. 4 angstroms/turn = 18. 9 angstroms. Note: full marks for 3 or 4 turns estimated.

Related Questions

Is it possible to make some predictions about protein secondary structure based on the primary sequence. Consider the following amino acid sequence: 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 Ile-Ala-His-Thr-Tyr-Gly-Pro-Phe-Glu-Ala-Ala-Met-Cys-Lys-Trp-Glu-Ala-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe-His-Arg A) Where might Beta-Turns occur? B) Where might intrachain disulfide cross-linkages be formed? C) Assuming that this sequence is part of a larger globular protein, what is the probable location (exterior or interior of the protein) of the amino acid residues: Asp Ile Thr Ala Gln Lys Explain your reasoning.

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