Christopher R. Travis
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View article: WDR5 Binding to Histone Serotonylation Is Driven by an Edge-Face Aromatic Interaction with Unexpected Electrostatic Effects.
WDR5 Binding to Histone Serotonylation Is Driven by an Edge-Face Aromatic Interaction with Unexpected Electrostatic Effects. Open
Histone serotonylation has emerged as a key post-translational modification. WDR5 preferentially binds to serotonylated histone 3 (H3), and this binding event has been associated with tumorigenesis. Herein, we utilize genetic code expansio…
View article: Stimulus-Induced Relief of Intentionally Incorporated Frustration Drives Refolding of a Water-Soluble Biomimetic Foldamer
Stimulus-Induced Relief of Intentionally Incorporated Frustration Drives Refolding of a Water-Soluble Biomimetic Foldamer Open
Frustrated, or nonoptimal, interactions have been proposed to be essential to a protein's ability to display responsive behavior such as allostery, conformational signaling, and signal transduction. However, the intentional incorporation o…
View article: The role of multivalency in the association of the eight twenty-one protein 2 (ETO2) with the nucleosome remodeling and deacetylase (NuRD) complex
The role of multivalency in the association of the eight twenty-one protein 2 (ETO2) with the nucleosome remodeling and deacetylase (NuRD) complex Open
Over the past 50 years, research has uncovered the co-regulatory proteins and complexes that silence the expression of the γ-globin gene in a developmental stage-specific manner. Recent research expanded the list of these regulatory factor…
View article: Abstract 3009 Differential Binding Preferences of Histone Trimethyllysine Reader Proteins Offers Promise for Therapeutic Design
Abstract 3009 Differential Binding Preferences of Histone Trimethyllysine Reader Proteins Offers Promise for Therapeutic Design Open
View article: Negative Cooperativity in the UHRF1 TTD‐PHD Dual Domain Masks the Contributions of Cation‐π Interactions between Trimethyllysine and the TTD Aromatic Cage
Negative Cooperativity in the UHRF1 TTD‐PHD Dual Domain Masks the Contributions of Cation‐π Interactions between Trimethyllysine and the TTD Aromatic Cage Open
UHRF1 is a promising epigenetic target in oncology, but inhibitor development has proven challenging due to the interplay between its tandem Tudor domain (TTD) and plant homeodomain (PHD). The TTD binds trimethyllysine (Kme3) at position 9…
View article: WDR5 Binding to Histone Serotonylation Is Driven by an Edge–Face Aromatic Interaction with Unexpected Electrostatic Effects
WDR5 Binding to Histone Serotonylation Is Driven by an Edge–Face Aromatic Interaction with Unexpected Electrostatic Effects Open
Histone serotonylation has emerged as a key post-translational modification. WDR5 preferentially binds to serotonylated histone 3 (H3), and this binding event has been associated with tumorigenesis. Herein, we utilize genetic code expansio…
View article: Contribution of Electrostatic CH<sub>3</sub>–π Interactions to Recognition of Histone Asymmetric Dimethylarginine by the SPIN1 Triple Tudor Domain
Contribution of Electrostatic CH<sub>3</sub>–π Interactions to Recognition of Histone Asymmetric Dimethylarginine by the SPIN1 Triple Tudor Domain Open
Methylation of arginine (Arg) residues on histones creates a new binding epitope, enabling recognition by aromatic cage binding pockets in Tudor domains; these protein-protein interactions (PPIs) govern gene expression. Despite their biolo…
View article: Trimethyllysine Reader Proteins Exhibit Widespread Charge-Agnostic Binding via Different Mechanisms to Cationic and Neutral Ligands
Trimethyllysine Reader Proteins Exhibit Widespread Charge-Agnostic Binding via Different Mechanisms to Cationic and Neutral Ligands Open
In the last 40 years, cation-π interactions have become part of the lexicon of noncovalent forces that drive protein binding. Indeed, tetraalkylammoniums are universally bound by aromatic cages in proteins, suggesting that cation-π interac…
View article: Probing the non-covalent forces key to the thermodynamics of β-hairpin unfolding
Probing the non-covalent forces key to the thermodynamics of β-hairpin unfolding Open
Per-residue analysis of the thermodynamics of unfolding of β-hairpins provides insight into the non-covalent interactions between residues, and the individual contributions of residues and secondary structure type to the Δ H , Δ S , and Δ …
View article: Stimulus-Induced Relief of Intentionally Incorporated Frustration Drives Refolding of a Water-Soluble Biomimetic Foldamer
Stimulus-Induced Relief of Intentionally Incorporated Frustration Drives Refolding of a Water-Soluble Biomimetic Foldamer Open
Frustrated, or nonoptimal, interactions have been proposed to be essential to a protein's ability to display responsive behavior such as allostery, conformational signaling, and signal transduction. However, the intentional incorporation o…
View article: Stimulus-Induced Relief of Intentionally Incorporated Frustration Drives Refolding of a Water-Soluble Biomimetic Foldamer
Stimulus-Induced Relief of Intentionally Incorporated Frustration Drives Refolding of a Water-Soluble Biomimetic Foldamer Open
Frustrated, or nonoptimal, interactions have been proposed to be essential to a protein’s ability to display responsive behav-ior, such as allostery, conformational signaling, and signal transduction. However, the intentional incorporation…
View article: Trimethyllysine reader proteins exhibit widespread charge-agnostic binding via different mechanisms to cationic and neutral ligands
Trimethyllysine reader proteins exhibit widespread charge-agnostic binding via different mechanisms to cationic and neutral ligands Open
In the last 40 years, cation−π interactions have become part of the lexicon of noncovalent forces that drive protein binding. Indeed, tetraalkylammoniums are universally bound by aromatic cages in proteins, suggesting that cation−π interac…
View article: Evaluation of acyllysine isostere interactions with the aromatic pocket of the <scp>AF9 YEATS</scp> domain
Evaluation of acyllysine isostere interactions with the aromatic pocket of the <span>AF9 YEATS</span> domain Open
Amide−π interactions, in which an amide interacts with an aromatic group, are ubiquitous in biology, yet remain understudied relative to other noncovalent interactions. Recently, we demonstrated that an electrostatically tunable amide−π in…
View article: More Than π–π–π Stacking: Contribution of Amide−π and CH−π Interactions to Crotonyllysine Binding by the AF9 YEATS Domain
More Than π–π–π Stacking: Contribution of Amide−π and CH−π Interactions to Crotonyllysine Binding by the AF9 YEATS Domain Open
Lysine crotonylation (Kcr) is a histone post-translational modification that is implicated in numerous epigenetic pathways and diseases. Recognition of Kcr by YEATS domains has been proposed to occur through intermolecular amide-π and alke…
View article: Genetic Encoding of a Bioconjugation Handle for [2+2+2] Cycloaddition Reactions
Genetic Encoding of a Bioconjugation Handle for [2+2+2] Cycloaddition Reactions Open
Protein bioconjugates have many critical applications, especially in the development of therapeutics. Consequently, the design of novel methodologies to prepare protein bioconjugates is of great importance. Herein we present the developmen…
View article: Mechanistic investigation and further optimization of the aqueous Glaser−Hay bioconjugation
Mechanistic investigation and further optimization of the aqueous Glaser−Hay bioconjugation Open
The Glaser–Hay bioconjugation has emerged as an efficient method to generate bioconjugates with therapeutic applications.
View article: Development and Optimization of Bioconjugations to Probe and Modulate Protein Function
Development and Optimization of Bioconjugations to Probe and Modulate Protein Function Open
Bioconjugate chemistry is a critical field with widespread applications to the visualization, diagnosis, and treatment of various diseases. Thus, it is crucial to investigate and optimize present bioconjugation methods, while continuing to…
View article: Utilization of alkyne bioconjugations to modulate protein function
Utilization of alkyne bioconjugations to modulate protein function Open