Prediction of folding equilibria of differently substituted peptides using 
one-step perturbation

Lin, Zhixiong; Kornfeld, Jörgen; Machler, Markus; van Gunsteren, Wilfred F.

doi:10.1021/ja100879k

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Prediction of folding equilibria of differently substituted peptides using one-step perturbation

MPS-Authors

There are no MPG-Authors in the publication available

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

Lin, Z., Kornfeld, J., Machler, M., & van Gunsteren, W. F. (2010). Prediction of folding equilibria of differently substituted peptides using one-step perturbation. Journal of the American Chemical Society, 132(21), 7276-7278. doi:10.1021/ja100879k.

Cite as: https://hdl.handle.net/21.11116/0000-0009-7648-2

Abstract

Computer simulation using long molecular dynamics (MD) can be used to simulate the folding equilibria of peptides and small proteins. However, a systematic investigation of the influence of the side-chain composition and position at the backbone on the folding equilibrium is computationally as well as experimentally too expensive because of the exponentially growing number of possible side-chain compositions and combinations along the peptide chain. Here, we show that application of the one-step perturbation technique may solve this problem, at least computationally; that is, one can predict many folding equilibria of a polypeptide with different side-chain substitutions from just one single MD simulation using an unphysical reference state. The methodology reduces the number of required separate simulations by an order of magnitude.