ch04-1 - Review question One method used to prevent...

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One method used to prevent disulfide bond interference with protein sequencing procedures is: A) cleaving proteins with proteases that specifically recognize disulfide bonds. B) protecting the disulfide bridge against spontaneous reduction to sulfhydryl (SH) groups. C) reducing disulfide bridges and preventing their re-formation by further modifying the —SH groups. D) removing cystines from protein sequences by proteolytic cleavage. E) sequencing proteins that do not contain disulfide bonds. Review question
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3-18 SDS-PAGE: sodium dodecyl sulfate polyacrylamide gel electrophoresis
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How many polypeptides does the purified protein (right lane) contain? 4
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3-27 Complete sequencing of (poly)peptides Long polypeptides must be cleaved into smaller, sequenceable fragments…
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Protein Structure Chapter 4 3-23
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Why is the α -helix conformation in polypeptides such a stable form? A. The α helix structure is stabilized by hydrophobic interactions. B. The α helix structure is stabilized by hydrogen bonds. C. The α helix structure is stabilized by disulfide bonds. D. The α helix structure is stabilized by proline residues.
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3-13
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4-2a Each peptide bond has a small electric dipole. Where does this come from? Partial negative Partial positive
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4-2 Which is the peptide bond? Are these cis or trans peptide bonds (with respect to carbonyl O and amide H)? trans (phi) = (psi) = 0°
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4-3 Ramachandran plot for L-Ala residues: allowed conformations in blue
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Secondary (2˚) Structures -helix -sheet
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4-4 5-6 Å -helix 1.5 Å/residue Stabilized by H-bonding between peptide groups; all aa H-bonded except near ends.
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4-4 -helix interactions (e.g. ionic, hydrophobic) between R groups can stabilize or destabilize helix formation.
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Box 4-1 Determining handedness of helices
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right- or left- handed? What about
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ch04-1 - Review question One method used to prevent...

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