Electrostatic interaction between dipoles and side chains in the voltage sensor domain of K(+) channel.

ABSTRACT:

Background

It is well known that α-helices of protein, possessing equal and opposite charged ends, behaves like a macrodipole, but the relative importance of such macrodipoles to the aggregation of a pair of helix in the voltage sensor domain (VSD) of K+ ion channel, has not been assessed. In the VSD, importance has been given primarily to the helically arranged Arginine residues of helix, but the role of the charged residues of S3b is less focused.

Method and objective

Applying electrostatic theory, we have studied the interaction between the charges of S3b-S4 α-helix pair of KvAP through virtual mutagenesis.

Result and conclusion

We have shown that the terminal charges arising from the inherent dipolar property of α-helices play an important role in affecting the st

SUBMITTER: Mapder T 

PROVIDER: S-EPMC3633302 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature