midterm_2_001_key

midterm_2_001_key - CHEM 237 Midterm 2 Tuesday November...

Info iconThis preview shows pages 1–3. Sign up to view the full content.

View Full Document Right Arrow Icon
CHEM 237 Midterm 2 Tuesday November 9 th , 2010 Name: ID: Instructions: Copy your version number into the test master box on the scantron, this is version 001 Fill in your ID number in the boxes on the scantron There are 9 pages including this cover sheet and 34 questions on this exam. Make sure you have a complete test booklet. You have 50 minutes to complete this exam. That includes copying your answers on to the scantron form. Useful? Information: ° = ±²³´ [ µ ] ¶² + [ · ] ¸ = 1 + [ ¹ ] ¶º
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Name: Page 2 of 9 1. What is true about methemoglobin? A. methemoglobin has methionine binding to the Fe 2+ instead of His. B. methemoglobin is a result of a single, specific mutation in the α 1 β 2-interface that results in oxidation of the iron to Fe 3+ . C. this form of Hb has a particularly high affinity for O 2 and does not release bound O 2 in the body. D. methemoglobin can be the result of any one of a number of mutations that result in the oxidation of the heme iron. E. None of the above 2. The sickle cell mutant, HbS causes physiological problems because A. the R- state dissociates into αβ dimers and loses all cooperativity. B. the R-state forms fibrils that disrupt the red blood cell. C. the T-state forms long fibers which disrupt the red blood cell membrane at lower pH. D. the “S” in HbS stands for “synthetic”; this variant was actually synthesized in the lab for research purposes and actually has no physiological effect. E. None of the above 3. Which of the following substitutions would you expect to disrupt the 3D structure of a protein the most? A. Ala Val in the hydrophobic core B. Glu Arg on the solvent exposed surface C. Gln Asn on the surface D. Thr Pro in an alpha helix E. Lys Arg in a buried network of H bonds 4. Which of the following statements is true? A. Some proteins requires chaperones like groEl and gro ES to fold properly. B. Hydrophobic collapse is usually the last step in protein folding. C. Once a protein has been denatured it can never refold. D. Protein folding causes the entropy of both the protein and the solvent to decrease E. Once a disulfide bond forms it cannot break and reform during protein folding 5. Which of the following statements regarding quaternary structures of proteins is correct? A. Quaternary structure is stabilized by hydrogen bonds between backbone carbonyl oxygens and amide hydrogens. B. Quaternary structure is determined solely by the interactions between secondary structure elements. C. Quaternary structure describes the interactions between different subunits in a multi subunit protein. D. Quaternary structure fully describes the folded conformation of a single polypeptide chain. E.
Background image of page 2
Image of page 3
This is the end of the preview. Sign up to access the rest of the document.

This note was uploaded on 12/02/2010 for the course CHEM 233 taught by Professor Daub during the Fall '09 term at Waterloo.

Page1 / 9

midterm_2_001_key - CHEM 237 Midterm 2 Tuesday November...

This preview shows document pages 1 - 3. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online