bis102-10-7

bis102-10-7 - 10/7/2011 Secondary structure of proteins...

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10/7/2011 Secondary structure of proteins random coil- flexible, changing, statistically random structure beta-sheet- 2 tyes 1. antiparallel 2. parallel hydrogen bonding between strands. all peptide linkages particiate. the R groups alternately project above and below the plane of the sheet. alpha helix- energetically feasible under certain conditions Beta sheet -- pleated. energetically feasible under certain conditions Ribbon models of proteins- often used to demonstrate the secondary structure characteristics of particular proteins Tertiary sturcture (III degrees) - folding, bending and convolution of a single polypeptide chain into a compact structure This folding brings R grps together from amino acid residues far away in the sequence . yields specific conformations of the protein that are thermodynamically most feasible. ultimate conformation that the protein takes. .. taking into consideration the R groups, backbone, etc. .. the most energetically favorable way to keep it stable. hydrophobic interactions- involved in the stabilization of tertiary structure
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This note was uploaded on 01/15/2012 for the course BIS 102 taught by Professor Hilt during the Fall '08 term at UC Davis.

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bis102-10-7 - 10/7/2011 Secondary structure of proteins...

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