Articles written in Journal of Chemical Sciences
Volume 119 Issue 5 September 2007 pp 545-552
We report here a theoretical study on the effect of electrostatic interactions on the formation of dynamical, proton-conducting hydrogen-bonded networks in the protein HCA II. The conformational fluctuations of His-64 is found to contribute crucially to the mechanism of such path formation irrespective of the way electrostatic interactions are modelled.
Volume 129 Issue 7 July 2017 pp 1031-1044 REGULAR ARTICLE
The mutant His-107-Tyr of human carbonic anhydrase II (HCA II) is highly unstable and has long been linked to a misfolding disease known as carbonic anhydrase deficiency syndrome (CADS). High temperature unfolding trajectories of the mutant are obtained from classical molecular dynamics simulationsand analyzed in a multi-dimensional property space.When projected along a reaction coordinate these trajectories yield four distinguishable sets of structures that map qualitatively to folding intermediates of this mutant postulated earlier from experiments.We present in this article a detailed analysis of representative structures and proton transfer activity of these intermediates. It is also suggested that under suitable experimental conditions, these intermediates may be distinguished using circular dichroism (CD) spectroscopy.
Volume 132, 2020
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