English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Assessing the stability of alanine-based helices by conformer-selective IR spectroscopy

Hoffmann, W., Marianski, M., Warnke, S., Seo, J., Baldauf, C., Helden, G. v., et al. (2016). Assessing the stability of alanine-based helices by conformer-selective IR spectroscopy. Physical Chemistry Chemical Physics, 18(29), 19950-19954. doi:10.1039/C6CP03827A.

Item is

Files

show Files
hide Files
:
c6cp03827a.pdf (Publisher version), 2MB
Name:
c6cp03827a.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
2016
Copyright Info:
This journal is©the Owner Societies

Locators

show

Creators

show
hide
 Creators:
Hoffmann, Waldemar1, 2, Author              
Marianski, Mateusz1, Author              
Warnke, Stephan1, Author              
Seo, Jongcheol1, Author              
Baldauf, Carsten3, Author              
Helden, Gert von1, Author              
Pagel, Kevin1, Author              
Affiliations:
1Molecular Physics, Fritz Haber Institute, Max Planck Society, ou_634545              
2Freie Universität Berlin, Takustraße 3, 14195 Berlin, Germany , ou_persistent22              
3Theory, Fritz Haber Institute, Max Planck Society, ou_634547              

Content

show
hide
Free keywords: -
 Abstract: Polyalanine based peptides that carry a lysine at the C-terminus ([Ac-AlanLys + H]+) are known to form α-helices in the gas phase. Three factors contribute to the stability of these helices: (i) the interaction between the helix macro dipole and the charge, (ii) the capping of dangling C=O groups by lysine and (iii) the cooperative hydrogen bond network. In previous studies, the influence of the interaction between the helix dipole and the charge as well as the impact of the capping was studied intensively. Here, we complement these findings by systematically assessing the third parameter, the H-bond network. In order to selectively remove one H-bond along the backbone, we use amide-to-ester substitutions. The resulting depsi peptides were analyzed by ion-mobility and m/z-selective infrared spectroscopy as well as theoretical calculations. Our results indicate that peptides which contain only one ester bond still maintain the helical conformation. We conclude that the interaction between the charge and the helix macro-dipole is most crucial for the formation of the α-helical conformation and a single backbone H-bond has only little influence on the overall stability.

Details

show
hide
Language(s):
 Dates: 2016-06-022016-07-042016-07-052016-08-07
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1039/C6CP03827A
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Physical Chemistry Chemical Physics
  Abbreviation : Phys. Chem. Chem. Phys.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Cambridge, England : Royal Society of Chemistry
Pages: 5 Volume / Issue: 18 (29) Sequence Number: - Start / End Page: 19950 - 19954 Identifier: ISSN: 1463-9076
CoNE: https://pure.mpg.de/cone/journals/resource/954925272413_1