BCH210H1 Lecture Notes - Lecture 3: Asparagine, Hemoglobin, Globular Protein
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BCH210H1 Full Course Notes
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Ch 2 (q 1(abc), 2(abc), 3, 4, 19b) Primary protein structure: secondary protein structure, tertiary protein structure, quaternary protein structure. Lecture 3/12 - intro to proteins and protein structure. Primary (1 ): linear aa sequence: secondary (2 ): periodic, repetitive units (alpha-helix, beta-sheet, reverse turn, tertiary (3 ): folding of secondary segments into defined protein structure, quaternary (4 ): assembly of protein sub-units. Example: insulin: this is an example of two linear structures bound together by disulfide bonds. Alpha chain and beta chain: amino acids are typically read from the n-terminus (nh end) to the c-terminus (cooh end) Here, the nh group of residue i donates h bond back to c=o group of reside i-4. H-bonds that form here are always in competition with water. Need to pack side chains and minimize the steric clashes --> this config does it. This is a right-handed helix --> most common in nature. This is a hydrophobic structure and is an enthalpy reaction.
