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Published byNathan Stuart Farmer Modified over 9 years ago
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Chapter 4.1: Overview of Protein Structure CHEM 7784 Biochemistry Professor Bensley
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CHAPTER 4.1 Overview of Protein Structure –The structure and properties of the peptide bond Today’s Objectives - To learn and understand:
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Structure of Proteins - Terms Conformation – spatial arrangement of atoms in a protein Native conformation – conformation of functional protein (also known as native fold)
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Favorable Interactions in Proteins Review: –Hydrophobic effect Release of water molecules from the structured solvation layer around the molecule as protein folds increases the net entropy –Hydrogen bonds Interaction of N-H and C=O of the peptide bond leads to local regular structures such as -helixes and -sheets –London dispersion Medium-range weak attraction between all atoms contributes significantly to the stability in the interior of the protein –Electrostatic interactions Long-range strong interactions between permanently charged groups Salt-bridges, esp. buried in the hydrophobic environment strongly stabilize the protein
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Structure of the Peptide Bond The peptide bond is a resonance hybrid of two canonical structures
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The Rigid Peptide Plane and the Partially Free Rotations Rotation around the peptide bond is not permitted Rotation around bonds connected to the alpha carbon is permitted
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Not all / Angles are Possible
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Distribution of and Dihedral Angles Ramachandran plot shows the distribution of and dihedral angles that are found in a protein shows the common secondary structure elements reveals regions with unusual backbone structure
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