Energetics of protein-protein interactions: Analysis ofthe Barnase-Barstar interface by single mutations and double mutant cycles

G Schreiber, AR Fersht - Journal of molecular biology, 1995 - Elsevier
The interaction of barnase, an extracellular RNase of Bacillus amyloliquefaciens, with its
intracellular inhibitor barstar is a suitable paradigm for protein-protein interactions, since the …

[引用][C] Energetics of protein-protein interactions: Analysis ofthe Barnase-Barstar interface by single mutations and double mutant cycles

G Schreiber, AR Fersht - Journal of Molecular Biology, 1995 - cir.nii.ac.jp
Energetics of protein-protein interactions: Analysis ofthe Barnase-Barstar interface by single
mutations and double mutant cycles | CiNii Research CiNii 国立情報学研究所 学術情報ナビゲータ …

Energetics of protein-protein interactions: Analysis ofthe Barnase-Barstar interface by single mutations and double mutant cycles

G Schreiber, AR Fersht - Journal of Molecular Biology, 1995 - weizmann.elsevierpure.com
The interaction of barnase, an extracellular RNase of Bacillus amyloliquefaciens, with its
intracellular inhibitor barstar is a suitable paradigm for protein-protein interactions, since the …

Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles

G Schreiber, AR Fersht - Journal of molecular biology, 1995 - pubmed.ncbi.nlm.nih.gov
The interaction of barnase, an extracellular RNase of Bacillus amylolique-faciens, with its
intracellular inhibitor barstar is a suitable paradigm for protein-protein interactions, since the …

Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles.

G Schreiber, AR Fersht - Journal of Molecular Biology, 1995 - europepmc.org
The interaction of barnase, an extracellular RNase of Bacillus amylolique-faciens, with its
intracellular inhibitor barstar is a suitable paradigm for protein-protein interactions, since the …

Energetics of protein-protein interactions: Analysis ofthe Barnase-Barstar interface by single mutations and double mutant cycles

G Schreiber, AR Fersht - Journal of Molecular Biology, 1995 - infona.pl
The interaction of barnase, an extracellular RNase of Bacillus amyloliquefaciens, with its
intracellular inhibitor barstar is a suitable paradigm for protein-protein interactions, since the …

[引用][C] ENERGETICS OF PROTEIN-PROTEIN INTERACTIONS: ANALYSIS OF THE BARNASE-BARSTAR INTERFACE BY SINGLE MUTATIONS AND DOUBLE …

G SCHREIBER, AR FERSHT - Journal of molecular biology, 1995 - Elsevier