bch 101 molecular graphics lab 1

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Biochem 101 Molecular Graphics Lab 1

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  • 1)

  • 1a)

  • 1b)

  • 1c)

  • 1d

  • 2a

  • 2cThis angle confirms my assignment of the hybridizations of my C. I assigned the C to be sp3 hybridized which will give it bond angles of approximately 109.5. The bond angle of this C is 109.0 which is very close to the ideal bond angle of an sp3 hybridized carbon. The slight variation in bond angle is most likely due to the interactions between the attachments to this carbon. C

  • 3aPerpendicular Parallel

  • 3bparallelperpendicular

  • 3cParallelPerpendicular

    This structure is an -helix.

  • 4a

  • 4b

  • 4cThe charged residues are located on the outer part and the neutral residues are located on the inside of the protein away from the solvent. The charged residues are able to be on the outside since they have polar areas, allowing them to interact with the polar water molecules. The neutral residues are non-polar and hydrophobic, therefore, they arrange themselves in the center of the protein, away from the polar solvent. The basic and acidic residues are charged, so they are sticking out from the protein exposed to the solvent. Because of their charged nature, it is easier for them to interact with the polar solvents which also has a slight polarity to it. The neutral residues are turned inward, hidden from the solvent. The neutral residues are all non-polar so they do not want to interact with the polar solvent. They face in towards the center of the protein which keeps them away from the polar solvent.

  • 5aThis specific peptide is held together in its helical shape due to hydrogen bonds (2.5A-3.1A) between a carbonyl group and an amide nitrogen 4 residues down the chain. These hydrogen bonds occur down the peptide creating the -helix structure.

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