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    STUDIA PHYSICA - Issue no. 2 / 2003  
         
  Article:   SECONDARY STRUCTURE ANALYSIS OF C-TERMINAL DOMAIN IN HUMAN CENTRIN 2 BY NMR SPECTROSCOPY AND CIRCULAR DICHROISM.

Authors:  ELENA MATEI, C.T. CRAESCU, P. DUCHAMBON, C. NICULESCU, Y. BLOUQUIT, S. SIMON.
 
       
         
  Abstract:  Analysis of two-dimensional NMR spectra recorded from isolated C-terminal domains of human centrine 2 (HCen2) offers information on the elements of its secondary structure. Five  helices (F89 - Q95, K103 –F113, F123 – E132, D139 – A149, E159 - K167) and an anti-parallel -sheet (K120-S122, E156-S158) are identified. The two EF-hand motifs form a canonical structure, similar to the “open” forms of other Ca2+-saturated regulatory domains. The structural stability and binding properties of HCen2 and its isolated domains are characterized using the circular dichroism spectroscopy. Comparative chemical stability studies reveal that the structure of the longer domain LC-HCen2 is considerably more stable than that of the shorter one SC-HCen2.  
         
     
         
         
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