AKProblemSet3

AKProblemSet3 - Practice Problem Set # 3 114A; 2006 1. Name...

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Practice Problem Set # 3 114A; 2006 1. Name the amino acids frequently seen in α -helices, β -strands and turns. Please look at Table 6-1 (a-helix prefers Ala, Glu, Leu, Lys; b-strands—val, Tyr; tyrn—Gly, Pro, Asp) 2. Discuss the potential contributions of hydrophobic and van der waals interactions and ionic and hydrogen bonds in the tertiary structure of a protein. Discuss how the following four amino acids, Asp, Leu, Tyr and His, can participate in the four types of interactions mentioned above maintain the tertiary structure. Hydrophobic interaction is the biggest contributor to protein folding allowing the proteins hydrophobic patch to be folded into the interior (which minimizes contact with water). Leucine will be in the interior and the other polar residues will be on the surface. In short distances, Wan der waals interaction stabilize protein; H-bonds fine tunes the folding by binding to specific residues at the required positions. Ion pairs also allow for correct folding and are usually on the surface of the protein. Tyrosine, Asparagine, and
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This note was uploaded on 01/31/2010 for the course CHEM chem 114A taught by Professor Gourisankarghosh during the Fall '06 term at UCSD.

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AKProblemSet3 - Practice Problem Set # 3 114A; 2006 1. Name...

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