Unknown

Dataset Information

0

Distinctive circular dichroism signature for 14-helix-bundle formation by beta-peptides.


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.

SUBMITTER: Pomerantz WC 

PROVIDER: S-EPMC2886586 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Distinctive circular dichroism signature for 14-helix-bundle formation by beta-peptides.

Pomerantz William C WC   Grygiel Tami L R TL   Lai Jonathan R JR   Gellman Samuel H SH  

Organic letters 20080409 9


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  ...[more]

Similar Datasets

| S-EPMC6712486 | biostudies-literature
| S-EPMC2724756 | biostudies-literature
| S-EPMC2736578 | biostudies-literature
| S-EPMC2752309 | biostudies-literature
| S-EPMC2744782 | biostudies-literature
| S-EPMC3928965 | biostudies-literature
| S-EPMC3950807 | biostudies-other