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Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions.
Pisabarro MT, Serrano L, Wilmanns M. Pisabarro MT, et al. Among authors: serrano l. J Mol Biol. 1998 Aug 21;281(3):513-21. doi: 10.1006/jmbi.1998.1932. J Mol Biol. 1998. PMID: 9698566
Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces.
Serrano L, Sancho J, Hirshberg M, Fersht AR. Serrano L, et al. J Mol Biol. 1992 Sep 20;227(2):544-59. doi: 10.1016/0022-2836(92)90906-z. J Mol Biol. 1992. PMID: 1404368
The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding.
Fersht AR, Matouschek A, Serrano L. Fersht AR, et al. Among authors: serrano l. J Mol Biol. 1992 Apr 5;224(3):771-82. doi: 10.1016/0022-2836(92)90561-w. J Mol Biol. 1992. PMID: 1569556 Review.
The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability.
Serrano L, Kellis JT Jr, Cann P, Matouschek A, Fersht AR. Serrano L, et al. J Mol Biol. 1992 Apr 5;224(3):783-804. doi: 10.1016/0022-2836(92)90562-x. J Mol Biol. 1992. PMID: 1569557 Review.
The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure.
Serrano L, Matouschek A, Fersht AR. Serrano L, et al. J Mol Biol. 1992 Apr 5;224(3):805-18. doi: 10.1016/0022-2836(92)90563-y. J Mol Biol. 1992. PMID: 1569558 Review.
The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure.
Matouschek A, Serrano L, Fersht AR. Matouschek A, et al. Among authors: serrano l. J Mol Biol. 1992 Apr 5;224(3):819-35. doi: 10.1016/0022-2836(92)90564-z. J Mol Biol. 1992. PMID: 1569559 Review.
The folding of an enzyme. V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies.
Matouschek A, Serrano L, Meiering EM, Bycroft M, Fersht AR. Matouschek A, et al. Among authors: serrano l. J Mol Biol. 1992 Apr 5;224(3):837-45. doi: 10.1016/0022-2836(92)90565-2. J Mol Biol. 1992. PMID: 1569560
The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models.
Serrano L, Matouschek A, Fersht AR. Serrano L, et al. J Mol Biol. 1992 Apr 5;224(3):847-59. doi: 10.1016/0022-2836(92)90566-3. J Mol Biol. 1992. PMID: 1569561
Effect of active site residues in barnase on activity and stability.
Meiering EM, Serrano L, Fersht AR. Meiering EM, et al. Among authors: serrano l. J Mol Biol. 1992 Jun 5;225(3):585-9. doi: 10.1016/0022-2836(92)90387-y. J Mol Biol. 1992. PMID: 1602471
Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles.
Serrano L, Bycroft M, Fersht AR. Serrano L, et al. J Mol Biol. 1991 Mar 20;218(2):465-75. doi: 10.1016/0022-2836(91)90725-l. J Mol Biol. 1991. PMID: 2010920
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