Density functional theory study of the conformational space of an infinitely 
long polypeptide chain

Ireta, Joel; Scheffler, Matthias

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Density functional theory study of the conformational space of an infinitely long polypeptide chain

MPS-Authors

/persons/resource/persons21661

Ireta, Joel
Theory, Fritz Haber Institute, Max Planck Society;

/persons/resource/persons22064

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

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Ireta, J., & Scheffler, M. (2009). Density functional theory study of the conformational space of an infinitely long polypeptide chain. Journal of Chemical Physics, 131(8), 085104-1-085104-5. Retrieved from http://www.fhi-berlin.mpg.de/th/th.html.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-F83F-D

Abstract

The backbone conformational space of infinitely long polyalanine is investigated with density-functional theory and mapping the potential-energy surface in terms of (L, θ) cylindrical coordinates. A comparison of the obtained (L, θ) Ramachandran-like plot with results from an extended set of protein structures shows excellent conformity, with the exception of the polyproline II region. It is demonstrated the usefulness of infinitely long polypeptide models for investigating the influence of hydrogen bonding and its cooperative effect on the backbone conformations. The results imply that hydrogen bonding together with long-range electrostatics is the main actuator for most of the structures assumed by protein residues.