about
Allostery in the LacI/GalR family: variations on a themeRheostats and toggle switches for modulating protein functionThermodynamics, protein modification, and molecular dynamics in characterizing lactose repressor protein: strategies for complex analyses of protein structure-function.Amino acid positions subject to multiple coevolutionary constraints can be robustly identified by their eigenvector network centrality scoresAlloRep: A Repository of Sequence, Structural and Mutagenesis Data for the LacI/GalR Transcription RegulatorsData on publications, structural analyses, and queries used to build and utilize the AlloRep database.Comparing the functional roles of nonconserved sequence positions in homologous transcription repressors: implications for sequence/function analyses.Comparison of simulated and experimentally determined dynamics for a variant of the Lacl DNA-binding domain, Nlac-P.Functionally important positions can comprise the majority of a protein's architecture.Modular, multi-input transcriptional logic gating with orthogonal LacI/GalR family chimeras.Multiple co-evolutionary networks are supported by the common tertiary scaffold of the LacI/GalR proteins.Linker regions of the RhaS and RhaR proteins.Flexibility and Disorder in Gene Regulation: LacI/GalR and Hox Proteins.Novel insights from hybrid LacI/GalR proteins: family-wide functional attributes and biologically significant variation in transcription repression.Allosteric transition pathways in the lactose repressor protein core domains: asymmetric motions in a homodimer.Fine-tuning function: correlation of hinge domain interactions with functional distinctions between LacI and PurRLigand-induced conformational changes and conformational dynamics in the solution structure of the lactose repressor proteinSubdividing repressor function: DNA binding affinity, selectivity, and allostery can be altered by amino acid substitution of nonconserved residues in a LacI/GalR homologue.Using Evolution to Guide Protein Engineering: The Devil IS in the Details.Functional consequences of exchanging domains between LacI and PurR are mediated by the intervening linker sequence.In vivo tests of thermodynamic models of transcription repressor function.Perturbation from a distance: mutations that alter LacI function through long-range effects.Computational predictors fail to identify amino acid substitution effects at rheostat positions.Using networks to identify fine structural differences between functionally distinct protein states.Integrated insights from simulation, experiment, and mutational analysis yield new details of LacI function.Resmap: automated representation of macromolecular interfaces as two-dimensional networks.Designed disulfide between N-terminal domains of lactose repressor disrupts allosteric linkage.RheoScale: A tool to aggregate and quantify experimentally determined substitution outcomes for multiple variants at individual protein positionsTemperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domainHydrogen bonds and the pH dependence of ovomucoid third domain stabilityLigand interactions with lactose repressor protein and the repressor-operator complex: the effects of ionization and oligomerization on bindingEnzymatic reaction sequences as coupled multiple traces on a multidimensional landscapeHomolog comparisons further reconcile in vitro and in vivo correlations of protein activities by revealing over-looked physiological factorsThe strengths and limitations of using biolayer interferometry to monitor equilibrium titrations of biomolecules
P50
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P50
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wetenschapper
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հետազոտող
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Liskin Swint-Kruse
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Liskin Swint-Kruse
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Liskin Swint-Kruse
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Liskin Swint-Kruse
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Liskin Kruse
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Liskin Swint-Kruse
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Liskin Swint-Kruse
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Liskin Swint-Kruse
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Liskin Swint-Kruse
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P106
P31
P496
0000-0002-5925-9741