Bacillus amyloliquefaciens ribonuclease

Known as: Bacillus amyloliquefaciens RNase, RNase ba, barnase 
 
National Institutes of Health

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Highly Cited
2011
Highly Cited
2011
Three-dimensional (3D) protein-patterned scaffolds provide a more biomimetic environment for cell culture than traditional two… (More)
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Highly Cited
2001
Highly Cited
2001
Atomic force microscopy (AFM) experiments have provided intriguing insights into the mechanical unfolding of proteins such as… (More)
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Highly Cited
1999
Highly Cited
1999
We report the computer generation of a high-density map of the thermodynamic properties of the diffusion-accessible encounter… (More)
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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… (More)
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Highly Cited
1995
Highly Cited
1995
The interaction of barnase, an extracellular RNase of Bacillus amylolique-faciens, with its intracellular inhibitor barstar is a… (More)
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Highly Cited
1993
Highly Cited
1993
Disulfide bridges have been introduced into barnase to act as probes of folding. One disulfide (between residues 85 and 102… (More)
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Review
1992
Review
1992
The structure of the first significant transition state on the unfolding pathway of barnase has been analysed in detail by… (More)
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Highly Cited
1990
Highly Cited
1990
Kinetic experiments on engineered mutants of barnase detect an intermediate on the folding pathway and allow the mapping of the… (More)
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Highly Cited
1990
Highly Cited
1990
Many of the interactions that stabilize proteins are co-operative and cannot be reduced to a sum of pairwise interactions. Such… (More)
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1987
1987
An inactivated gene for Bacillus amyloliquefaciens extracellular ribonuclease (barnase) has previously been cloned and sequenced… (More)
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