Ch2-2 - folding Alpha Helices are Formed by n to n+4...

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Buffers Regulate pH ] [ ] [ log HA A pH pK a - - = ] [ ] [ log HA A pK pH a - + = or Henderson-Hasselbach Equation
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7 Sidechains and 2 Termini Contain Ionizable groups
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Zwitterionic Form of Amino Acids in  Solution
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3 Letter and 1 Letter aa Codes
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Primary Structure: Residues Connected by a kinetically stable peptide bond to form the backbone of a polypeptide chain. The polypeptide has polarity . R=Side Chains Main chain (backbone) H-bond donor H-bond acceptor 50-2000 aa/protein
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The Peptide Bond has Restricted Flexibility Essentially planar, double bond character,
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Steric Factors Favor Trans over cis Bonds Proline is Different
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Definition of φ , ψ, and the  Ramachandran Plot Restricted rotations facilitate
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Unformatted text preview: folding Alpha Helices are Formed by n to n+4 Backbone Hydrogen Bonds (predicted by Pauling and Corey) 3.6 residues/turn Pitch 5.4 Schematic Representations of Alpha Helices Ferritin, a helical protein A Coiled Coil 75% helical Up to 100 nM Beta Strand Antiparallel Beta Sheet Parallel Beta Sheet Rise ~ 3.5 A Mixed Beta Sheet A Twisted Beta Sheet 3.5 angstroms between aa (vs. 1.5 in helix) 4-5-10 or more strands per sheet Structurally more diverse Fatty acid binding protein Turns and Loops add to Diversity on Protein Secondary Structures Reverse Turn or Turn Loops...
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Ch2-2 - folding Alpha Helices are Formed by n to n+4...

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