English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The modeling of voltage-gated ion-channel proteins is a continuing challenge for force-field calculations because of the diverse range of interactions involved. In particular, current force fields are not parameterized for either ion]amino acid or amino acid]electric field interactions. To address the parameterization of ion]amino acid interactions, we have tested the use of empirical correction terms, derived from ab initio calculations of single amino Ž . q acids representing the peptide backbone interacting with K ions. Having demonstrated the utility of such an approach, we then extended the application to the amino acid side chains. The calculation of the interaction of Kq with Ž . serine, cysteine, methionine, lysine, arginine, aspartate, histidine uncharged , tyrosine, tryptophan, and phenylalanine, both completes the parameterization of the molecular environments contained in the amino acids, and allows specific comment on these ion]functional group interactions. The cation]p interactions were of particular interest, given recent proposals in the literature and the fear that force fields would not be able to treat such interactions. We present a Ž w x . comprehensive comparison of the ab initio DFT BLYP , 6-311 G** and force Ž . field CHARMm22.0 assessments of these interactions. Q 1998 John Wiley & Sons, Inc. J Comput Chem 19: 1515]1525, 1998

j. comput. chem.

Development of modified force field for cation-amino acid interactions: Ab initio-derived empirical correction terms with comments on cation- interactions