Gurunath, R and Balaram, P (1995) A Nonhelical, Multiple beta-Turn Conformation in a Glycine-Rich Heptapeptide Fragment of Trichogin A IV Containing a Single Central alpha-Aminoisobutyric Acid Residue. In: Biopolymers, 35 (1). pp. 21-29.
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The conformational properties of the protected seven-residue C-terminal fragment of the lipo-peptaibol antibiotic Trichogin A IV (Boc-Gly-Gly-Leu-Aib-Gly-Ile-Leu-OMe) has been examined in CDC13 and (CD3),S0 by 'H-nmr. Evidence for a multiple beta-turn conformation [type I' at Gly(l)-Gly(2), type II at Leu(3)-Aib(4). and a type I' at Aib(4)-Gly(S)] suggests that Leu (3) has preferred an extended or semiextended conformation over a helical conformation in CDCl3. This structure is thus in contrast to earlier observations of seven-residue peptides containing a single central Aib preferring helical conformations in both solution and crystalline states. A structural transition to a frayed right-handed helix is observed in (CD3)2SO. These results suggest that nonhelical conformations may be important in Gly-rich peptides containing Aib. Further, the presence of amino acids with contradictory influences on backbone conformational freedom can lead to well-defined conformational transitions even in small peptides.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to John Wiley & Sons, Inc.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||09 Nov 2004|
|Last Modified:||19 Sep 2010 04:17|
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