Staff Publications

Staff Publications

  • external user (warningwarning)
  • Log in as
  • language uk
  • About

    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

    We have a manual that explains all the features 

Record number 431077
Title Ligand binding and conformational states of photoprotein obelin
Author(s) Eremeeva, E.; Vysotski, E.S.; Westphal, A.H.; Mierlo, C.P.M. van; Berkel, W.J.H. van
Source FEBS Letters 586 (2012)23. - ISSN 0014-5793 - p. 4173 - 4179.
DOI http://dx.doi.org/10.1016/j.febslet.2012.10.015
Department(s) Biochemistry
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2012
Keyword(s) recombinant obelin - crystal-structure - light-emission - apo-aequorin - bioluminescence - coelenterazine - luminescence - stability - angstrom - proteins
Abstract Many proteins require a non-covalently bound ligand to be functional. How ligand binding affects protein conformation is often unknown. Here we address thermal unfolding of the free and ligand-bound forms of photoprotein obelin. Fluorescence and far-UV circular dichroism (CD) data show that the various ligand-dependent conformational states of obelin differ significantly in stability against thermal unfolding. Binding of coelenterazine and calcium considerably stabilizes obelin. In solution, all obelin structures are similar, except for apo-obelin without calcium. This latter protein is an ensemble of conformational states, the populations of which alter upon increasing temperature.
Comments
There are no comments yet. You can post the first one!
Post a comment
 
Please log in to use this service. Login as Wageningen University & Research user or guest user in upper right hand corner of this page.