BIO 361 Lecture Notes - Lecture 8: Chaotropic Agent, Protein Folding, Hydrophobe
27 Jun 2016
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Biochemistry professor sanford simon stony brook summer 2016. The hydrophobic effect has the greatest influence on protein stability. Folded proteins are only 0. 4 kj mol-1 residue-1 more stable than unfolded proteins. The greater the hydrophobicity of a side chain, the greater the chance of it being buried in the protein interior. Hydropathy plot allows prediction of hydrophobic and hydrophilic side chains of amino acid residues. Van der waals interactions are important in the interior of proteins. Hydrogen bonds make only minor contributions to protein stability but are important for defining the protein folding pathway. Salt bridges are found on the exterior of proteins but are rarely conserved. High temperatures require additional salt bridges for the strong interaction. Alpha-helix is an arrangement that allows for maximal hydrogen bonds. Zinc is coordinated by a wide range of protein side. Zinc finger motifs are found in dna binding proteins.
