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Synthetic and conformational studies on dehydrophenylalanine containing model peptides

✍ Scribed by KAUR, PARAMJEET ;UMA, K. ;BALARAM, P. ;CHAUHAN, V.S.

Book ID
115098859
Publisher
Wiley (Blackwell Publishing)
Year
2009
Tongue
English
Weight
490 KB
Volume
33
Category
Article
ISSN
0367-8377

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📜 SIMILAR VOLUMES

Synthetic and conformational studies on
Synthetic and conformational studies on dehydroalanine-containing model peptides
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Three model dipeptides containing a dehydroalanine residue ( AAla) at the C-terminal, Boc-X-AAla-NHCH3 [ X = Ala, Val, and Phe,] have been synthesized and their solution conformations investigated by 'H-NMR, IR, and CD spectroscopy. NMR studies on these peptides in CDCl, clearly indicate that the NH

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Fourier transform ir spectra have been recorded for three 3 10 -helical and one ␣-helical pentapeptides containing dehydrophenylalanine, in a thin solid film, in order to find marker bands for various secondary structures encountered in peptides containing dehydroaminoacids. The peptide solutions we

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## Abstract Synthesis and conformational studies of a cecropin–melittin hybrid pentadecapeptide CA(1–7)MEL(2–9), and its three α, β‐dehydrophenylalanine (ΔPhe) containing analogs in water‐TFE mixtures are described. ΔPhe is placed at strategic positions in order to preserve the amphipathicity of th

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## Abstract The conformational behavior of POE‐bound model peptides Boc‐(L‐Ala)~2~‐X‐Y‐(L‐Ala)~2~‐NHPOE (X – Y = L‐Pro‐Gly (**I**), Gly‐L‐Ile (**II**); NHPOE = aminopoly(oxyethylene)) as well as of the repetitive hexapeptide of elastin, Boc‐L‐Val‐L‐Ala‐L‐Pro‐Gly‐L‐Val‐Gly‐A‐NHPOE‐M (**III**) (A = p