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Journal of Molecular Biology|September 24, 1999
GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helicesJ Chatellier, A M Buckle, A R FershtBiochemistry|February 22, 1994
Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolutionA M Buckle, A R FershtJournal of Molecular Biology|December 22, 2000
From minichaperone to GroEL 1: information on GroEL-polypeptide interactions from crystal packing of minichaperonesQ Wang, A M Buckle, A R FershtBiochemistry|August 2, 1994
Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolutionA M Buckle, G Schreiber, A R FershtJournal of Molecular Biology|December 22, 2000
From minichaperone to GroEL 2: importance of avidity of the multisite ring structureJ Chatellier, F Hill, A R FershtJournal of Molecular Biology|December 5, 1993
Crystal structural analysis of mutations in the hydrophobic cores of barnaseA M Buckle, K Henrick, A R FershtJournal of Molecular Biology|May 10, 2000
Stabilization of GroEL minichaperones by core and surface mutationsQ Wang, A M Buckle, A R FershtStructure (London, England : 1993)|October 15, 1994
Stability and function: two constraints in the evolution of barstar and other proteinsG Schreiber, A M Buckle, A R FershtBiochemistry|April 9, 1996
Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavitiesA M Buckle, P Cramer, A R FershtProceedings of the National Academy of Sciences of the United States of America|April 15, 1997
A structural model for GroEL-polypeptide recognitionA M Buckle, R Zahn, A R FershtPageof 34