1,514 research outputs found
Experimental Study of Parametric Autoresonance in Faraday Waves
The excitation of large amplitude nonlinear waves is achieved via parametric
autoresonance of Faraday waves. We experimentally demonstrate that phase
locking to low amplitude driving can generate persistent high-amplitude growth
of nonlinear waves in a dissipative system. The experiments presented are in
excellent agreement with theory.Comment: 4 pages, 4 eps figures, to appear in Phys. Rev. Let
Probing the Evaporation Dynamics of Ethanol/Gasoline Biofuel Blends Using Single Droplet Manipulation Techniques
Peer reviewedPublisher PD
A Critical Examination of Contemporary Legal Issues Important to College Presidents
This discussion provides a highlight of the legal dimensions that college presidents must consider in providing oversight for college operations. Many of these issues are driven by the behaviors of campus constituents, but several key legal issues are also the result of federal legislation and involvement in higher education
Effects of Art Intervention on Pediatric Anxiety and Pain in the Medical Setting
Introduction: Hospitalization and illness can be a painful and stressful time for a child. There may be anxiety over procedures and inpatient stays disrupt normal routines. Previous research found that for pre-school aged children, having parents around, having the help of the hospital staff, and playing an active role in alleviating their fears were the most helpful in reducing anxiety. Another study found that visual creative expressions can be meaningful experiences for young adult cancer survivors. Additionally, there is abundant literature on formal art therapy and its favorable effects on children in the hospital, however, there are fewer studies investigating less standardized “art intervention” in the same population. The purpose of our project was to assess whether art intervention reduces anxiety and pain in inpatient and outpatient pediatric patients.https://scholarworks.uvm.edu/comphp_gallery/1224/thumbnail.jp
Mechanistic Heterogeneity in Site Recognition by the Structurally Homologous DNA-Binding Domains of the ETS-Family Transcription Factors Ets-1 and PU.1
ETS-family transcription factors regulate diverse genes through binding at cognate DNA sites that overlap substantially in sequence. The DNA-binding domains of ETS proteins (ETS domains) are highly conserved structurally, yet share limited amino acid homology. To define the mechanistic implications of sequence diversity within the ETS family, we characterized the thermodynamics and kinetics of DNA site recognition by the ETS domains of Ets-1 and PU.1, which represent the extremes in amino acid divergence among ETS proteins. Even though the two ETS domains bind their optimal sites with similar affinities under physiologic conditions, their nature of site recognition differs strikingly in terms of the role of hydration and counter-ion release. The data suggest two distinct mechanisms wherein Ets-1 follows a “dry” mechanism that rapidly parses sites through electrostatic interactions and direct protein-DNA contacts, while PU.1 utilizes hydration to interrogate sequence-specific sites and form a long-lived complex relative to the Ets-1 counterpart. The kinetic persistence of the high-affinity PU.1/DNA complex may be relevant to an emerging role of PU.1, but not Ets-1, as a pioneer transcription factor in vivo. In addition, PU.1 activity is critical to the development and function of macrophages and lymphocytes, which present osmotically variable environments, and hydrationdependent specificity may represent an important regulatory mechanism in vivo, a hypothesis that finds support in gene expression profiles of primary murine macrophages
Mechanistic Heterogeneity in Site Recognition by the Structurally Homologous DNA-Binding Domains of the ETS-Family Transcription Factors Ets-1 and PU.1
ETS-family transcription factors regulate diverse genes through binding at cognate DNA sites that overlap substantially in sequence. The DNA-binding domains of ETS proteins (ETS domains) are highly conserved structurally, yet share limited amino acid homology. To define the mechanistic implications of sequence diversity within the ETS family, we characterized the thermodynamics and kinetics of DNA site recognition by the ETS domains of Ets-1 and PU.1, which represent the extremes in amino acid divergence among ETS proteins. Even though the two ETS domains bind their optimal sites with similar affinities under physiologic conditions, their nature of site recognition differs strikingly in terms of the role of hydration and counter-ion release. The data suggest two distinct mechanisms wherein Ets-1 follows a “dry” mechanism that rapidly parses sites through electrostatic interactions and direct protein-DNA contacts, while PU.1 utilizes hydration to interrogate sequence-specific sites and form a long-lived complex relative to the Ets-1 counterpart. The kinetic persistence of the high-affinity PU.1/DNA complex may be relevant to an emerging role of PU.1, but not Ets-1, as a pioneer transcription factor in vivo. In addition, PU.1 activity is critical to the development and function of macrophages and lymphocytes, which present osmotically variable environments, and hydrationdependent specificity may represent an important regulatory mechanism in vivo, a hypothesis that finds support in gene expression profiles of primary murine macrophages
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