Hierarchy of local structural and dynamics perturbations due to subdenaturing urea in the native state ensemble of DLC8 dimer

Krishna Mohan, P. M. ; Chakraborty, Swagata ; Hosur, Ramakrishna V. (2010) Hierarchy of local structural and dynamics perturbations due to subdenaturing urea in the native state ensemble of DLC8 dimer Biophysical Chemistry, 153 (1). pp. 17-26. ISSN 0301-4622

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/j.bpc.2010.09.010

Abstract

Local structural and dynamic modulations due to small environmental perturbations reflect the adaptability of the protein to different interactors. We have investigated here the preferential local perturbations in Dynein light chain protein (DLC8), a cargo adapter, by sub-denaturing urea concentrations. Equilibrium unfolding experiments by optical spectroscopic methods indicated a two state like unfolding of DLC8 dimer, with the transition mid-point occurring around 8.6 M urea. NMR studies identified the β3 and β4 strands, N-, C- terminal regions, loops connecting β1 to α1, α1 to α2 and β3 to β4 as the soft targets of urea perturbation and thus indicated potential unfolding initiation sites. Native-state hydrogen exchange studies suggested the unfolding to traverse from the edges towards the centre of the secondary structural elements. At 6 M urea the whole protein chain acts like a cooperative unit. These observations are expected to have important implications for the protein's multiple functions.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Dynein Light Chain Protein (DLC8); Nuclear Magnetic Resonance; Equilibrium States; Unfolding Mechanism; Circular Dichroism; Fluorescence Spectroscopy
ID Code:80106
Deposited On:31 Jan 2012 04:21
Last Modified:31 Jan 2012 04:21

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