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The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure.
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The folding of an enzyme VI. The folding pathway of barnase: Comparison with theoretical models
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<title>Energy transfer and specific fluorescence quenching effects in barnase, studied via multifrequency phase-fluorometry of tryptophan mutants</title>
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Surface electrostatic interactions contribute little to stability of barnase
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Pathway and stability of protein folding.
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COSMIC analysis of the major alpha-helix of barnase during folding.
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Aromatic-aromatic interactions and protein stability
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218
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Linear free energy relationships in enzyme binding interactions studied by protein engineering
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STABILIZATION OF BARNASE BY AN INTERACTION BETWEEN 2 OPPOSITELY CHARGED SIDE-CHAINS
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Strength and co-operativity of contributions of surface salt bridges to protein stability
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Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins
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