Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bpc.2013.02.005
Title: Structural study of hNck2 SH3 domain protein in solution by circular dichroism and X-ray solution scattering
Authors: Matsumura, Y.
Shinjo, M.
Matsui, T.
Ichimura, K.
Song, J. 
Kihara, H.
Keywords: C-state
Equilibrium helix-rich intermediate
Monomer-dimer transition
Issue Date: May-2013
Citation: Matsumura, Y., Shinjo, M., Matsui, T., Ichimura, K., Song, J., Kihara, H. (2013-05). Structural study of hNck2 SH3 domain protein in solution by circular dichroism and X-ray solution scattering. Biophysical Chemistry 175-176 : 39-46. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bpc.2013.02.005
Abstract: We have done conformational study of hNck2 SH3 domain by means of far-ultraviolet (far-UV) circular dichroism (CD) and X-ray solution scattering (XSS). The results indicated that the following: (1) hNck2 SH3 domain protein exhibited concentration dependent monomer-dimer transition at neutral pH, while the secondary structure of this protein was independent of the protein concentration. (2) The hNck2 SH3 domain also exhibited pH dependent monomer-dimer transition. This monomer-dimer transition was accompanied with helix-β transition of the secondary structural change. Moreover, the acid-induced conformation, which was previously studied by Liu and Song by CD and nuclear magnetic resonance (NMR), was found to be not compact, but the conformation of the protein at acidic pH was similar to the cold denatured state (C-state) reported by Yamada et al. for equine β-lactoglobulin. We calculated that a structure of the equilibrium helix-rich intermediate of the hNck2 SH3 domain by DAMMIF program. © 2013 Elsevier B.V.
Source Title: Biophysical Chemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/101766
ISSN: 03014622
DOI: 10.1016/j.bpc.2013.02.005
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