English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Conference Paper

How mono-valent cations bend peptide turns and a first-principles database of amino acids and dipeptides

MPS-Authors
/persons/resource/persons21325

Baldauf,  Carsten
Theory, Fritz Haber Institute, Max Planck Society;

/persons/resource/persons22025

Ropo,  Matti
Theory, Fritz Haber Institute, Max Planck Society;
Department of Physics, Tampere University of Technology;
COMP, Department of Applied Physics, Aalto University;

/persons/resource/persons21379

Blum,  Volker
Theory, Fritz Haber Institute, Max Planck Society;
Duke University, MEMS Department, Durham, NC 27708, USA;

/persons/resource/persons22064

Scheffler,  Matthias
Theory, Fritz Haber Institute, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Baldauf, C., Ropo, M., Blum, V., & Scheffler, M. (2014). How mono-valent cations bend peptide turns and a first-principles database of amino acids and dipeptides. In T. E. Simos, Z. Kalogiratou, & T. Monovasilis (Eds.), Proceedings of the International Conference of Computational Methods in Sciences and Engineering 2014: (ICCMSE 2014) (pp. 119-120). Melville, NY: AIP Publishing.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-97F4-8
Abstract
In this contribution we detail our efforts to investigate the structural effects of cations binding to peptides and amino acids. We perform first-principles studies employing long-range dispersion-corrected approximate density-functional theory and compare to gas-phase experiments.