Thermodynamic Characterization of the Reversible, Two-State Unfolding of Maltose Binding Protein, a Large Two-Domain Protein†

Biochemistry ◽  
1997 ◽  
Vol 36 (16) ◽  
pp. 5020-5028 ◽  
Author(s):  
C. Ganesh ◽  
Aseema N. Shah ◽  
C. P. Swaminathan ◽  
Avadhesha Surolia ◽  
Raghavan Varadarajan
2009 ◽  
Vol 31 (11) ◽  
pp. 1677-1684 ◽  
Author(s):  
Min Han ◽  
In Su Park ◽  
Soo Hyun Kim ◽  
Byung Soo Kim ◽  
Sang-Heon Kim

2010 ◽  
Vol 38 (12) ◽  
pp. 2239-2245 ◽  
Author(s):  
Robert R. Reddy ◽  
Erik C. Ralph ◽  
Meike S. Motika ◽  
Jun Zhang ◽  
John R. Cashman

2000 ◽  
Vol 182 (24) ◽  
pp. 7078-7082 ◽  
Author(s):  
Kunitoshi Yamanaka ◽  
Jihwan Hwang ◽  
Masayori Inouye

ABSTRACT A gene encoding a putative GTP-binding protein, a TrmE homologue that is highly conserved in both prokaryotes and eukaryotes, was cloned from Thermotoga maritima, a hyperthermophilic bacterium.T. maritima TrmE was overexpressed in Escherichia coli and purified. TrmE has a GTPase activity but no ATPase activity. The GTPase activity can be competed with GTP, GDP, and dGTP but not with GMP, ATP, CTP, or UTP. Km andk cat at 70°C were 833 μM and 9.3 min−1, respectively. Our results indicate that TrmE is a GTP-binding protein with a very high intrinsic GTP hydrolysis rate. We also propose that TrmE homologues constitute a novel subfamily of the GTPase superfamily.


1993 ◽  
Vol 175 (18) ◽  
pp. 5762-5768 ◽  
Author(s):  
M A Goldstein ◽  
M Takagi ◽  
S Hashida ◽  
O Shoseyov ◽  
R H Doi ◽  
...  

Neuroscience ◽  
1999 ◽  
Vol 94 (2) ◽  
pp. 637-649 ◽  
Author(s):  
W.J. Rushlow ◽  
N. Rajakumar ◽  
B.A. Flumerfelt ◽  
C.C.G. Naus

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