Structural Insights into the Recovery of Aldolase Activity inN-Acetylneuraminic Acid Lyase by Replacement of the Catalytically Active Lysine with γ-Thialysine by Using a Chemical Mutagenesis Strategy

PROPKA3: Consistent Treatment of Internal and Surface Residues in Empirical pKaPredictions

(2011) Mats H. M. Olsson et al.   Journal of Chemical Theory and Computation

Methods for converting cysteine to dehydroalanine on peptides and proteins

(2011) Justin M. Chalker et al.   Chemical Science

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Optimizing non-natural protein function with directed evolution

(2010) Eric M Brustad et al.   CURRENT OPINION IN CHEMICAL BIOLOGY

Structural Insights into Substrate Specificity in Variants of N-Acetylneuraminic Acid Lyase Produced by Directed Evolution

(2010) Ivan Campeotto et al.   JOURNAL OF MOLECULAR BIOLOGY

Computational Design of an Enzyme Catalyst for a Stereoselective Bimolecular Diels-Alder Reaction

(2010) J. B. Siegel et al.   SCIENCE

Structure of anEscherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 Å resolution

(2009) Ivan Campeotto et al.   Acta Crystallographica Section F-Structural Biology and Crystallization Communications

Directed evolution of aldolases for exploitation in synthetic organic chemistry

(2008) Amanda Bolt et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Kemp elimination catalysts by computational enzyme design

(2008) Daniela Röthlisberger et al.   NATURE

De Novo Computational Design of Retro-Aldol Enzymes

(2008) L. Jiang et al.   SCIENCE

Chemical-modification rescue assessed by mass spectrometry demonstrates that γ-thia-lysine yields the same activity as lysine in aldolase

(2002) Christopher E. Hopkins et al.   PROTEIN SCIENCE