Louis Y P Luk

Affiliations: 
Cardiff University, Cardiff, Wales, United Kingdom 
Area:
Biocatalysis
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"Louis Luk"
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Publications

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Galmés MÀ, Nödling AR, Luk L, et al. (2021) Combined Theoretical and Experimental Study to Unravel the Differences in Promiscuous Amidase Activity of Two Nonhomologous Enzymes. Acs Catalysis. 11: 8635-8644
Allemann RK, Adresina AS, Luk L. (2021) Cryo-kinetics reveal dynamic effects on the chemistry of human dihydrofolate reductase. Chembiochem : a European Journal of Chemical Biology
Scott AF, Cresser-Brown J, Williams TL, et al. (2019) Crystal Structure and Biophysical Analysis of Furfural Detoxifying Aldehyde Reductase from . Applied and Environmental Microbiology
Allemann RK, Scott AF, Luk LY, et al. (2019) Heavy enzymes and the rational redesign of protein catalysts. Chembiochem : a European Journal of Chemical Biology
Allemann RK, Ruiz-Pernia JJ, Luk L, et al. (2018) Isotope substitution of promiscuous alcohol dehydrogenase reveals origin of substrate preference in transition state. Angewandte Chemie (International Ed. in English)
Loveridge EJ, Hroch L, Hughes RL, et al. (2017) Reduction of Folate by Dihydrofolate Reductase from Thermotoga maritima. Biochemistry
Castillo JP, Sánchez-Rodríguez JE, Hyde HC, et al. (2016) β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel. Proceedings of the National Academy of Sciences of the United States of America
Luk LY, Ruiz-Pernía JJ, Adesina AS, et al. (2015) Chemical Ligation and Isotope Labeling to Locate Dynamic Effects during Catalysis by Dihydrofolate Reductase. Angewandte Chemie (International Ed. in English). 54: 9016-20
Luk LY, Loveridge EJ, Allemann RK. (2015) Protein motions and dynamic effects in enzyme catalysis. Physical Chemistry Chemical Physics : Pccp. 17: 30817-27
Luk LY, Ruiz-Pernía JJ, Dawson WM, et al. (2014) Protein isotope effects in dihydrofolate reductase from Geobacillus stearothermophilus show entropic-enthalpic compensatory effects on the rate constant. Journal of the American Chemical Society. 136: 17317-23
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