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Chem 481 HW 1 - Homework Assignment 1 Chem 481 F10 Name...

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Homework Assignment 1 Chem 481 F10 Name ___________________________ Problems from text: 9. 11. 1. If you had the primary structure of a polypeptide chain and the individual Ψ and Φ angles on either side of the α -carbon of each amino acid residue, would you have enough information to accurately determine the complete 3 o structure of the polypeptide? Briefly justify your answer. 2. A Rhamachandran plot predicts that only certain values of Ψ and Φ are allowed for peptide backbones containing amino acids other than Gly and Pro. Briefly explain why these angles are limited and why Gly and Pro are different. 3. Both collagen and α -keratin are two important filamentous structural proteins that display a regular helical structure. Briefly describe the basic structural features of each and the principle forces that contribute to the stability of each. α -keratin collagen Helix type of single polypeptide chain Not Applicable Twist of single helix (handedness) Twist of basic multi-chain unit (handedness)
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4. The hydrophobic effect is the most important inter/intramolecular force in determining a protein’s native conformation. Explain what the hydrophobic effect is and how it helps determine the native conformation of a globular protein. 5. Briefly outline the molecular basic for each of these physiological aspects of hemoglobin function. Hill effect: Bohr effect: Rapid (within hours) adaptation to altitude changes: 6. The condition known as sickle cell anemia results from a single base change on the DNA strand the codes for one of the subunits of hemoglobin and results in several individual hemoglobin molecules “sticking” together. Briefly outline molecular the molecular differences between sickle cell and normal hemoglobin and how these differences are responsible for this medical condition.
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