In:
FEBS Letters, Wiley, Vol. 281, No. 1-2 ( 1991-04-09), p. 240-244
Abstract:
The structure and dynamic properties of bee venom molittin and a synthetic analogue. [Ala 14 ]‐melittin (melittin P14A), are compared, using high resolution 1 H nuclear magnetic resonance (NMR) spectroscopy and amide exchange measurements in methanol. P14A is shown to adopt a regular, stable α‐helical conformation in solution without the flexibility around the Pro‐14 residue found in melittin. P14A has twice the hemolytic activity of melittin but is less able to induce voltage‐dependent ion conductance in planar bilayers. The results indicate that helix flexibility afforded by the Pro‐14 residue promotes the ability of melittin to adopt the transbilayer associates thought to underlie ion translocation.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(91)80402-O
Language:
English
Publisher:
Wiley
Publication Date:
1991
detail.hit.zdb_id:
1460391-3
SSG:
12
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