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ABSTRACT:
SUBMITTER: Matsumura Y
PROVIDER: S-EPMC3925460 | biostudies-literature | 2013 May-Jun
REPOSITORIES: biostudies-literature
Matsumura Yoshitaka Y Shinjo Masaji M Matsui Tsutomu T Ichimura Kaoru K Song Jianxing J Kihara Hiroshi H
Biophysical chemistry 20130226
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 wa ...[more]