Skip to search formSkip to main contentSkip to account menu

Bacillus amyloliquefaciens ribonuclease

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

Related topics

Related topics

2 relations
Pancreatic ribonuclease

Broader (1)

Ribonucleases

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2001
2001
Salt Bridges Stabilize the Folded Structure of Barnase
Formation of salt bridges entails desolvation, and whether they stabilize protein structures is an open question. In this paper… 
1998
1998
Baculovirus-mediated gene transfer into mammalian cells
A klnd of cytotoxinic gene barnase was cloned downstream of Immediate early promoter from cytomegalovirus (CMV). Rerombinant… 
Highly Cited
1995
Highly Cited
1995
A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.
The denatured states of barnase that are induced by urea, acid, and high temperature and acid have been assigned and… 
Review
1994
Review
1994
Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions.
Assumptions about the dependence of protein unfolding on the concentration of urea have been examined by an extensive survey of… 
1993
1993
Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways.
We have measured the rate constants for exchange of amide protons in 15N-labeled wild-type barnase and a disulfide mutant that is… 
Highly Cited
1992
Highly Cited
1992
The folding of an enzyme. V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies.
Highly Cited
1992
Highly Cited
1992
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate.
Highly Cited
1991
Highly Cited
1991
Crystal structure of a barnase-d(GpC) complex at 1.9 A resolution.
Highly Cited
1990
Highly Cited
1990
Detection and characterization of a folding intermediate in barnase by NMR
PROTEIN engineering is being developed for mapping the energetics and pathway of protein folding. From kinetic studies on wild… 
Highly Cited
1972
Highly Cited
1972
Amino-acid sequence of extracellular ribonuclease (barnase) of Bacillus amyloliquefaciens.
THE ribonuclease, barnase, produced by Bacillus amyloliquefaciens has a molecular weight of 12,382, consisting of 110 amino-acid… 
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)