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barstar protein, Bacillus amyloliquefaciens

Known as: Nuclease inhibitor, barstar, barstar 
 
National Institutes of Health

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Highly Cited
2001
Highly Cited
2001
Theoretical and experimental studies have shown that the large desolvation penalty required for polar and charged groups… Expand
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Highly Cited
2001
Highly Cited
2001
We used a novel charge optimization technique to study the small ribonuclease barnase and to analyze its interaction with a… Expand
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Highly Cited
2000
Highly Cited
2000
The role of desolvation in protein binding kinetics is investigated using Brownian dynamics simulations in complexes in which the… Expand
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Highly Cited
1998
Highly Cited
1998
The electrostatic enhancement of the association rate of barnase and barstar is calculated using a transition-state theory like… Expand
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Highly Cited
1997
Highly Cited
1997
The rate of protein association places an upper limit on the response time due to protein interactions, which, under certain… Expand
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Highly Cited
1995
Highly Cited
1995
TWO models are commonly used to describe the poorly understood earliest steps of protein folding. The framework model1-3 stresses… Expand
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Highly Cited
1995
Highly Cited
1995
Isothermal guanidine hydrochloride (GdnHCl)-induced denaturation curves obtained at 14 different temperatures in the range 273… Expand
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Highly Cited
1994
Highly Cited
1994
We have solved, refined, and analyzed the 2.0-å resolution crystal structure of a 1:1 complex between the bacterial ribonuclease… Expand
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Highly Cited
1994
Highly Cited
1994
BACKGROUND Barstar is the intracellular inhibitor of barnase, an extracellular RNAse of Bacillus amyloliquefaciens. The… Expand
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Highly Cited
1993
Highly Cited
1993
Barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens, forms a very tight complex with its intracellular… Expand
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