worksheet 2

worksheet 2 - Worksheet 2 Secondary Structure: -helix and...

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Worksheet 2 1 Secondary Structure : α-helix and β strands, motifs Common structural patterns that arise from favorable interactions between amino acid residues. The entire molecule is made of one polypeptide chain, but certain regions will bond with itself or each other and form these secondary structures. What structures are formed depends on energetics. Certain residues show favorability for either structure. Alpha Helices: φ: ψ: 3.6 residues per turn, a new residue every 100˚ Stabilized by intra-strand H-bonds between C=O of residue n and N-H of n+4 . More loosely coiled ____ helix and more tightly coiled ____ helix are not energetically favorable. Good α-Helix formers: ____ ____ ____ ____ Why? Bad α-Helix formers: ____ ____ ____ ____ Why? Amphipathic helix: Alternating hydrophobic and hydrophilic side chains every 3-4 residues. Draw the Dipole moment Draw a Helical wheel: of an alpha helix: : Not all polypeptides can form alpha-helices. Side chain interactions (ex. Repulsion) – similar residues (of the same
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This note was uploaded on 04/23/2008 for the course BIBC 100 taught by Professor Nehring during the Fall '07 term at UCSD.

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worksheet 2 - Worksheet 2 Secondary Structure: -helix and...

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