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Journal Abstract Search

300 related items for PubMed ID: 11302708

  • 1. Experimental assignment of the structure of the transition state for the association of barnase and barstar.
    Frisch C, Fersht AR, Schreiber G.
    J Mol Biol; 2001 Apr 20; 308(1):69-77. PubMed ID: 11302708
    [Abstract] [Full Text] [Related]

  • 2. Thermodynamics of the interaction of barnase and barstar: changes in free energy versus changes in enthalpy on mutation.
    Frisch C, Schreiber G, Johnson CM, Fersht AR.
    J Mol Biol; 1997 Apr 04; 267(3):696-706. PubMed ID: 9126847
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  • 5. Optimization of binding electrostatics: charge complementarity in the barnase-barstar protein complex.
    Lee LP, Tidor B.
    Protein Sci; 2001 Feb 04; 10(2):362-77. PubMed ID: 11266622
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  • 6. On the dynamic nature of the transition state for protein-protein association as determined by double-mutant cycle analysis and simulation.
    Harel M, Cohen M, Schreiber G.
    J Mol Biol; 2007 Aug 03; 371(1):180-96. PubMed ID: 17561113
    [Abstract] [Full Text] [Related]

  • 7. Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution.
    Buckle AM, Schreiber G, Fersht AR.
    Biochemistry; 1994 Aug 02; 33(30):8878-89. PubMed ID: 8043575
    [Abstract] [Full Text] [Related]

  • 8. Structural response to mutation at a protein-protein interface.
    Vaughan CK, Buckle AM, Fersht AR.
    J Mol Biol; 1999 Mar 12; 286(5):1487-506. PubMed ID: 10064711
    [Abstract] [Full Text] [Related]

  • 9. The role of Glu73 of barnase in catalysis and the binding of barstar.
    Schreiber G, Frisch C, Fersht AR.
    J Mol Biol; 1997 Jul 04; 270(1):111-22. PubMed ID: 9231905
    [Abstract] [Full Text] [Related]

  • 10. Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering.
    Schreiber G, Fersht AR.
    Biochemistry; 1993 May 18; 32(19):5145-50. PubMed ID: 8494892
    [Abstract] [Full Text] [Related]

  • 11. How optimal are the binding energetics of barnase and barstar?
    Wang T, Tomic S, Gabdoulline RR, Wade RC.
    Biophys J; 2004 Sep 18; 87(3):1618-30. PubMed ID: 15345541
    [Abstract] [Full Text] [Related]

  • 12. Simulation of the diffusional association of barnase and barstar.
    Gabdoulline RR, Wade RC.
    Biophys J; 1997 May 18; 72(5):1917-29. PubMed ID: 9129797
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  • 13. The kinetics of protein-protein recognition.
    Janin J.
    Proteins; 1997 Jun 18; 28(2):153-61. PubMed ID: 9188733
    [Abstract] [Full Text] [Related]

  • 14. Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar.
    Guillet V, Lapthorn A, Hartley RW, Mauguen Y.
    Structure; 1993 Nov 15; 1(3):165-76. PubMed ID: 16100951
    [Abstract] [Full Text] [Related]

  • 15. Directed mutagenesis and barnase-barstar recognition.
    Hartley RW.
    Biochemistry; 1993 Jun 15; 32(23):5978-84. PubMed ID: 8507637
    [Abstract] [Full Text] [Related]

  • 16. Diffusional encounter of barnase and barstar.
    Spaar A, Dammer C, Gabdoulline RR, Wade RC, Helms V.
    Biophys J; 2006 Mar 15; 90(6):1913-24. PubMed ID: 16361332
    [Abstract] [Full Text] [Related]

  • 17. Protein-protein interaction: a genetic selection for compensating mutations at the barnase-barstar interface.
    Jucovic M, Hartley RW.
    Proc Natl Acad Sci U S A; 1996 Mar 19; 93(6):2343-7. PubMed ID: 8637875
    [Abstract] [Full Text] [Related]

  • 18. Stability and function: two constraints in the evolution of barstar and other proteins.
    Schreiber G, Buckle AM, Fersht AR.
    Structure; 1994 Oct 15; 2(10):945-51. PubMed ID: 7866746
    [Abstract] [Full Text] [Related]

  • 19. Force spectroscopy of barnase-barstar single molecule interaction.
    Sekatskii SK, Favre M, Dietler G, Mikhailov AG, Klinov DV, Lukash SV, Deyev SM.
    J Mol Recognit; 2010 Oct 15; 23(6):583-8. PubMed ID: 21038358
    [Abstract] [Full Text] [Related]

  • 20. Barnase-Barstar: from first encounter to final complex.
    Hoefling M, Gottschalk KE.
    J Struct Biol; 2010 Jul 15; 171(1):52-63. PubMed ID: 20211732
    [Abstract] [Full Text] [Related]

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