BCH210H1 Lecture Notes - Lecture 9: Protein Structure Prediction, Alpha Helix, Protein Folding

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BCH210H1 Full Course Notes
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BCH210H1 Full Course Notes
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The structure of a protein is defined by its primary structure. Proteins may be made up of alpha helices, beta sheets, beta turns or disordered regions: disordered regions are important for protein function. The tertiary structure is the final folded structure of a protein, but some proteins have quaternary structures. Proteins may exist in different structural conformations which allow them to carry out their function. Covalent and non-covalent interactions mediate these changes. There are 3 allowed conformation states defined by the five angles. Consider a polypeptide of 100 amino acids, where every amino acid has at least 3 conformations. Each conformation is sampled once in 10-13 seconds, it would take 1027 years for a protein to fold. Experimentally, when a protein is synthesized in the ribosome, it takes 0. 1-1000 seconds to fold. Folding is directed through specific folding pathways. Hydrogen bonds are important for secondary structure.

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