(Q49187978)

19 February 2018

title

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

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19 February 2018

protein-protein interaction

main subject

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2

Fersht AR

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19 February 2018

Schreiber G

1

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19 February 2018

language of work or name

English

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publication date

1 April 1995

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19 February 2018

Journal of Molecular Biology

published in

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19 February 2018

volume

248

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19 February 2018

page(s)

478-486

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19 February 2018

issue

2

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19 February 2018

Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution

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1 reference

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Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution

7 January 2021

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Amino-aromatic interactions in proteins

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Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy

7 January 2021

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The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)

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Comparison of a structural and a functional epitope

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Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis

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The sixth Datta Lecture. Protein folding and stability: the pathway of folding of barnase

7 January 2021

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Fine structure-activity analysis of mutations at position 51 of tyrosyl-tRNA synthetase

7 January 2021

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Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships

7 January 2021

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The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding

7 January 2021

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Calculation of protein extinction coefficients from amino acid sequence data

7 January 2021

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Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar.

7 January 2021

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Barnase and barstar: two small proteins to fold and fit together

7 January 2021

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Directed mutagenesis and barnase-barstar recognition.

7 January 2021

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Non-additivity in protein-protein interactions

7 January 2021

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Co-operative interactions during protein folding.

7 January 2021

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Protein-protein interactions: additivity of the free energies of association of amino acid residues.

7 January 2021

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Strength and co-operativity of contributions of surface salt bridges to protein stability

7 January 2021

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Contribution of long-range electrostatic interactions to the stabilization of the catalytic transition state of the serine protease subtilisin BPN'

7 January 2021

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7 January 2021

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Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability

7 January 2021

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Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy

7 January 2021

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Molecular structure of a new family of ribonucleases

7 January 2021

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Effect of active site residues in barnase on activity and stability

7 January 2021

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Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis

7 January 2021

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Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering

7 January 2021

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5'-3' exonucleases in phosphorothioate-based oligonucleotide-directed mutagenesis

7 January 2021

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Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering

7 January 2021

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The refolding of cis- and trans-peptidylprolyl isomers of barstar

7 January 2021

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Stability and function: two constraints in the evolution of barstar and other proteins

7 January 2021

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Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles

7 January 2021

1 reference

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The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability

7 January 2021

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Additivity of mutational effects in proteins

7 January 2021

1 reference

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10.1016/S0022-2836(95)80064-6

7 January 2021

Identifiers

DOI

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19 February 2018

PubMed ID

7739054

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19 February 2018