Growth, Thermal and Spectroscopic Characteristics of Nd3+:LiBi(MoO4)2 Crystal

2011 ◽  
Vol 25 (12) ◽  
pp. 1307-1312 ◽  
Author(s):  
Xin-Yang HUANG
2021 ◽  
Vol 272 ◽  
pp. 115331
Author(s):  
M. Nasri ◽  
C. Henchiri ◽  
R. Dhahri ◽  
J. Khelifi ◽  
H. Rahmouni ◽  
...  

2009 ◽  
Vol 57 (24) ◽  
pp. 11469-11475 ◽  
Author(s):  
Diana Agrelli ◽  
Carmine Amalfitano ◽  
Pellegrino Conte ◽  
Laura Mugnai

1990 ◽  
Vol 22 (S1) ◽  
pp. S133-S139 ◽  
Author(s):  
V. G. Ostroumov ◽  
I. A. Shcherbakov ◽  
E. V. Zharikov ◽  
Ch. Pfistner ◽  
P. Albers ◽  
...  

1993 ◽  
Vol 295 (2) ◽  
pp. 493-500 ◽  
Author(s):  
P Dominici ◽  
P S Moore ◽  
C Borri Voltattorni

The effect of guanidinium chloride (GuCl) on enzyme activity, hydrodynamic volume, circular dichroism, and fluorescence of 3,4-dihydroxyphenylalanine (Dopa) decarboxylase from pig kidney (pkDDC) was studied under equilibrium conditions. Unfolding proceeds in at least three stages. The first transition, occurring between 0 and 1 M GuCl, gives rise to a dimeric inactive species which has lost pyridoxal 5′-phosphate (PLP), and has a high tendency to aggregate, but retains almost all of the native spectroscopic characteristics. The second equilibrium transition, between 1 and 2.2 M GuCl, involves dimer dissociation, with some loss of tertiary and secondary structure. Additionally, gross conformational changes at or near the PLP microenvironment were detected by fluorescence of NaBH4-reduced enzyme. The third step, presumably representing complete unfolding of pkDDC, appears to be complete at 4.5 M GuCl, as indicated by the lack of further substantial changes in any of the signals being studied. Attempts at refolding resulted in the findings that: (1) partial reactivation is observed only starting from enzyme denatured at concentrations below 1.5 M GuCl, and (2) starting from completely denatured protein, the refolding process is apparently reversible down to concentrations of approx. 2 M GuCl. Taken together, this would seem to indicate that the monomer-dimer transition is impaired under the experimental conditions tested. A plausible model is presented for the unfolding/refolding of pkDDC.


1981 ◽  
Vol 86 (3) ◽  
pp. 194-198 ◽  
Author(s):  
A. Ranfagni ◽  
D. Mugnai ◽  
R. Englman

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