LSCI 211 Lecture Notes - Lecture 5: Proline, Alanine, Heteromer
28 Aug 2016
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Document Summary
The sequence of amino acids in a protein. Has the chemical information for the secondary and tertiary structure. Written from the n terminal (amino end) to c terminal (carboxyl end) Amino acids are held together by peptide bonds. Does not allow for rotation (due to double bond) Can be right-handed (globular, membrane, fibrous) or left-handed (fibrous) Commonly includes alanine, but proline and glycine disrupt the helix. Structure influenced by ph and presence of bulky amino acids. Positive dipoles towards the amino end, negative ones towards the carboxyl end. In parallel sheets, h-bonded strands run in the same direction. In antiparallel sheets, h-bonded strands run in the opposite direction. Link segments of - pleated sheets and - helices. Proline or glycine causes kinks in the amino acid chain. Overall spatial arrangement of atoms in a protein. Folding of a protein in on itself to hide hydrophobic residues from aqueous solvent. A super structure formed by association of multiple polypeptide chains.
