Abstract:
:A conformational transition is described for the polypeptide, gramicidin A, in which a dimer that forms a left-handed intertwined antiparallel helix is converted to a single-stranded amino terminus to amino terminus right-handed helix. The starting structure is determined here by solution NMR methods while reference is made to the well-established folding motif of gramicidin in a lipid bilayer for the ultimate conformation of this transition. Furthermore, an organic solvent system of benzene and ethanol in which gramicidin has a unique conformation is identified. This conformation is shown to be very similar to that derived from X-ray diffraction of crystals prepared from a similar solvent system.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Zhang Z,Pascal SM,Cross TAdoi
10.1021/bi00152a019subject
Has Abstractpub_date
1992-09-22 00:00:00pages
8822-8issue
37eissn
0006-2960issn
1520-4995journal_volume
31pub_type
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