| Literature DB >> 23524290 |
Yoshitaka Matsumura1, Masaji Shinjo, Tsutomu Matsui, Kaoru Ichimura, Jianxing Song, Hiroshi Kihara.
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.Entities:
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Year: 2013 PMID： 23524290 PMCID： PMC3925460 DOI： 10.1016/j.bpc.2013.02.005
Source DB: PubMed Journal: Biophys Chem ISSN： 0301-4622 Impact factor: 2.352