yeast enolase
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ACS Catalysis ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 8985-8990 ◽  
Author(s):  
Pengfei Li ◽  
Sharon Hammes-Schiffer


2011 ◽  
Vol 179 (1) ◽  
pp. 8-17 ◽  
Author(s):  
Sujaan Das ◽  
Saudamini Shevade ◽  
Douglas J. LaCount ◽  
Gotam K. Jarori


FEBS Letters ◽  
2010 ◽  
Vol 584 (5) ◽  
pp. 979-983 ◽  
Author(s):  
John M. Brewer ◽  
Jared S. McKinnon ◽  
Robert S. Phillips
Keyword(s):  


FEBS Journal ◽  
2007 ◽  
Vol 275 (1) ◽  
pp. 97-106 ◽  
Author(s):  
Songping Zhao ◽  
Bonny S. F. Choy ◽  
Mary J. Kornblatt


PROTEOMICS ◽  
2006 ◽  
Vol 6 (S1) ◽  
pp. S107-S118 ◽  
Author(s):  
Elena López-Villar ◽  
Lucía Monteoliva ◽  
Martin R. Larsen ◽  
Emmanuelle Sachon ◽  
Mohammed Shabaz ◽  
...  
Keyword(s):  


2004 ◽  
Vol 271 (19) ◽  
pp. 3897-3904 ◽  
Author(s):  
M. Judith Kornblatt ◽  
Reinhard Lange ◽  
Claude Balny


2003 ◽  
Vol 17 (2-3) ◽  
pp. 453-467 ◽  
Author(s):  
Ping Huang ◽  
Aichun Dong

We studied the temperature‒ and denaturant‒induced denaturation of yeast enolase by means of Fourier transform infrared spectroscopy. The temperature‒induced denaturation/aggregation of the enzyme in the absence of denaturant was highly cooperative and occurred between 55 and 65°C with a midpoint of ~58°C. Above 55°C, the intensity at 1656 cm−1(predominantly α‒helix) decreases as a function of temperature, accompanied by the appearance of two new bands at 1622 and 1696 cm−1, indicating the formation of intermolecular β‒sheet aggregates. Five clearly defined isosbestic points were observed, indicating a two‒state conformational transition. Addition of a non‒denaturing concentration of gdnHCl (0.4 M) caused the thermal denaturation/aggregation of the enzyme to proceed faster, but this revealed no unfolding intermediate. The gdnHCl‒induced unfolding was first detected at a gdnHCl concentration of above 0.4 M, evidenced by loss of α‒helix and β‒sheet structures as functions of denaturant concentration. The fully unfolded state was reached at a gdnHCl concentration of 1.6 M. A significant amount of intermolecular β‒sheet aggregate was detected at gdnHCl concentrations between 0.6 and 1.0 M, which disappeared as the denaturant concentration increased further. The gdnHCl‒unfolded state is a heterogeneous ensemble of turns, helix/loops, and random structures, which continues to change at higher concentrations of denaturant.



2000 ◽  
Vol 276 (3) ◽  
pp. 1199-1202 ◽  
Author(s):  
John M. Brewer ◽  
Michael J. Holland ◽  
Lukasz Lebioda


Biochemistry ◽  
1999 ◽  
Vol 38 (37) ◽  
pp. 12138-12149 ◽  
Author(s):  
Dmitriy A. Vinarov ◽  
Thomas Nowak
Keyword(s):  


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