Search Results - "Sorgenfrei, Frieda A."
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1
Boronate affinity electrophoresis for the purification and analysis of cofactor-modified RNAs
Published in Methods (San Diego, Calif.) (15-03-2017)“…•Boronic acid-modified polyacrylamide gels retard NAD-RNA compared to unmodified RNAs.•In vitro transcribed NAD-RNA can be purified on boronic acid-modified…”
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2
Solvent concentration at 50% protein unfolding may reform enzyme stability ranking and process window identification
Published in Nature communications (26-06-2024)“…As water miscible organic co-solvents are often required for enzyme reactions to improve e.g., the solubility of the substrate in the aqueous medium, an enzyme…”
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3
Kinome‐Wide Profiling Prediction of Small Molecules
Published in ChemMedChem (20-03-2018)“…Extensive kinase profiling data, covering more than half of the human kinome, are available nowadays and allow the construction of activity prediction models…”
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4
Kinetic and structural roles for the surface in guiding SAS-6 self-assembly to direct centriole architecture
Published in Nature communications (26-10-2021)“…Discovering mechanisms governing organelle assembly is a fundamental pursuit in biology. The centriole is an evolutionarily conserved organelle with a…”
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5
The dynamic properties of a nuclear coactivator binding domain are evolutionarily conserved
Published in Communications biology (30-03-2022)“…Evolution of proteins is constrained by their structure and function. While there is a consensus that the plasticity of intrinsically disordered proteins…”
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6
Transmembrane Shuttling of Photosynthetically Produced Electrons to Propel Extracellular Biocatalytic Redox Reactions in a Modular Fashion
Published in Angewandte Chemie International Edition (04-10-2022)“…Many biocatalytic redox reactions depend on the cofactor NAD(P)H, which may be provided by dedicated recycling systems. Exploiting light and water for…”
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7
Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins
Published in The Journal of biological chemistry (18-12-2020)“…Intrinsically disordered protein domains often have multiple binding partners. It is plausible that the strength of pairing with specific partners evolves from…”
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8
PQQ‐dependent Dehydrogenase Enables One‐pot Bi‐enzymatic Enantio‐convergent Biocatalytic Amination of Racemic sec‐Allylic Alcohols
Published in ChemCatChem (05-03-2021)“…The asymmetric amination of secondary racemic allylic alcohols bears several challenges like the reactivity of the bi‐functional substrate/product as well as…”
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9
Folding Optimization In Vivo Uncovers New Chaperones
Published in Journal of molecular biology (11-09-2015)“…By employing a genetic selection that forces the cell to fold an unstable, aggregation-prone test protein in order to survive, we have generated bacterial…”
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10
Transmembrane Shuttling of Photosynthetically Produced Electrons to Propel Extracellular Biocatalytic Redox Reactions in a Modular Fashion
Published in Angewandte Chemie (04-10-2022)“…Many biocatalytic redox reactions depend on the cofactor NAD(P)H, which may be provided by dedicated recycling systems. Exploiting light and water for…”
Get full text
Journal Article -
11
Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins
Published in The Journal of biological chemistry (18-12-2020)“…Intrinsically disordered protein domains often have multiple binding partners. It is plausible that the strength of pairing with specific partners evolves from…”
Get full text
Journal Article -
12
Cover Feature: PQQ‐dependent Dehydrogenase Enables One‐pot Bi‐enzymatic Enantio‐convergent Biocatalytic Amination of Racemic sec‐Allylic Alcohols (5/2021)
Published in ChemCatChem (05-03-2021)“…The Cover Feature picture shows an assembly line as a cartoon for the biocatalytic cascade described in the Communication by S. Gandomkar et al. The racemic…”
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13
Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins
Published in The Journal of biological chemistry (18-12-2020)“…Intrinsically disordered protein domains often have multiple binding partners. It is plausible that the strength of pairing with specific partners evolves from…”
Get full text
Journal Article