September 10

September 10 - September 10, 2010 Beta sheet Laterally...

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September 10, 2010 Beta sheet Laterally packed beta strands o Beta strand = short, 5-8 residues, nearly extended polypeptide segment H-bonding between backbone of the beta strand Same type of hydrogen bonding as alpha helix between amide hydrogen and carbonyl oxygen Forms a plane or a sheet within the protein R groups extend above and below the sheet alternatingly The sheet appears to be corrugated, or pleated when viewed from the side Beta strands can run parallel (running in the same direction N to C) or antiparallel (running in opposite directions N to C and C to N) Tertiary Structure the overall folding of a polypeptide long range folding within a polypeptide chain stabilized by hydrophobic interactions between nonpolar side chains, hydrogen bonds between polar side chains and disulfide bonds between cysteine residues provides a compact structure of alpha helices, beta sheets and turns hydrophobic residues (primary structure) tend to cluster inside the overall folded structure in an attempt to avoid contact with the polar solvent polar, charged, hydrophilic side chains tend to arrange themselves on the outside of the folded structure o these tendencies to find the right environment drives the overall folding of a polypeptide chain Motifs of Protein of secondary structure stereotypic arrangement of a polypeptide chain Coiled coil o
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This note was uploaded on 10/23/2010 for the course BIOL BIOL 200 taught by Professor Bureau during the Fall '09 term at McGill.

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September 10 - September 10, 2010 Beta sheet Laterally...

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