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Distinctive circular dichroism signature for 14-helix-bundle formation by beta-peptides.
- Source :
-
Organic letters [Org Lett] 2008 May 01; Vol. 10 (9), pp. 1799-802. Date of Electronic Publication: 2008 Apr 09. - Publication Year :
- 2008
-
Abstract
- We identify a distinctive circular dichroism (CD) signature for self-assembled 14-helical beta-peptides. Our data show that self-assembly leads to a mimimum at 205 nm, which is distinct from the well-known minimum at 214 nm for a monomeric 14-helix. The onset of assembly is indicated by [theta]205/[theta]214>0.7. Our results will facilitate rapid screening for self-assembling beta-peptides and raise the possibility that far-UV CD will be useful for detecting higher-order structure for other well-folded oligoamide backbones.
- Subjects :
- Protein Structure, Secondary
Circular Dichroism
Peptides chemistry
Protein Folding
Subjects
Details
- Language :
- English
- ISSN :
- 1523-7060
- Volume :
- 10
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Organic letters
- Publication Type :
- Academic Journal
- Accession number :
- 18396884
- Full Text :
- https://doi.org/10.1021/ol800622e