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By Nicholas Sperelakis

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Extra info for Cell Physiology Source Book. A Molecular Approach

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E, the structure of melittin has been computed (Fig. 9) and determined by x-ray crystallography with good agreement between the two structures. The structure of this protein may be thought of as a bent a-helical rod with a-helices from Gly 1 to Thr 10, a reverse turn at Thr 11 to Gly 12, followed by another ahelix from Pro 14 to Gin 26. Leu 13 can adopt an energetically favorable conformation, a D state (see Fig. 8) that results in a compact structure for the monomeric state. In the x-ray structure of tetrameric melittin, this residue adopts an energetically less favorable a-helical conformation, causing it to adopt a more open, "straight" structure.

The sequence of melittin is +H-Gly-Ile-Gly-Ala-Val-LeuLys-Val-Leu-Thr-Thr-Gly-Leu-Pro-Ala-Leu-Ile- S er-TrpIle-Lys-Arg-Lys-Arg-Gln-Gln-NH2. Inspection of this sequence reveals that this protein contains six positive charges and no negative charges. At least half of the residues are hydrophobic, as would be expected for a membrane-intercalating protein. E, the structure of melittin has been computed (Fig. 9) and determined by x-ray crystallography with good agreement between the two structures. The structure of this protein may be thought of as a bent a-helical rod with a-helices from Gly 1 to Thr 10, a reverse turn at Thr 11 to Gly 12, followed by another ahelix from Pro 14 to Gin 26.

0, the buffering of the NH 2 is maximal. The buffering capacity is governed by the Henderson-Hasselbalch equation, (5) H2N - CH 2 - COOFIGURE 11. Titration curve for a dibasic acid like glycine to show the two buffering regions for the COOH and NH~ groups and the isoelectric point that can be computed as (PKal + PK2)/2. A protein has multiple buffering regions, characteristic of each residue type that is involved in a prototropic dissociation. pH - p K + log [ conjugatebase form] [acidform] (3) where the pKa is the negative logarithm of the proton dis sociation constant for the acid.

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