Selection of abstracts from Baylor Scott & White Health Central Texas Scholars Day.

Baylor Scott & White Health Central Texas displayed the diversity and growth of scholarly pursuits during Scholars Day, which debuted online on May 6, 2022. Residents and fellows, medical students, nurses, and research staff were among those showcasing their scholarly activity in areas such as medical innovation, clinical vignettes, research, and quality improvement. A selection committee chose 34 abstracts-16 select podium, 18 rapid fire.

Selection of abstracts from Baylor Scott & White Health Central Texas Scholars Day.

Baylor Scott & White Health Central Texas displayed the diversity and growth of scholarly pursuits during Scholars Day, which debuted online on May 7, 2021. Residents and fellows, medical students, nurses, and research staff were among those showcasing their scholarly activity in areas such as medical innovation, clinical vignettes, research, and quality improvement. A selection of Scholar Day abstracts is presented here.

Selection of abstracts from Baylor Scott & White Health Central Texas Scholars Day.

Baylor Scott & White Health Central Texas displayed the diversity and growth of scholarly pursuits during Scholars Day on May 3, 2019. Residents and fellows, medical students, nurses, and research staff were among those showcasing their scholarly activity in areas such as medical innovation, clinical vignettes, research, and quality improvement. A selection committee chose 32 abstracts-12 select podium, 20 rapid fire.

Impact of health care adversity on providers: Lessons learned from a staff support program.

Background: Health care providers often experience traumatic events and adversity that can have negative emotional impacts on the profession and on patients. These impacts are typically multifaceted and can result from many different events, such as unanticipated outcomes, licensing board complaints, claims, and litigation. Because health care providers are exposed to diverse situations, they require adequate and timely support, imperative for provider resilience and patient safety.

Detailed microscopic unfolding pathways of an α-helix and a β-hairpin: direct observation and molecular dynamics.

We present a combined experimental and computational study of unfolding pathways of a model 21-residue α-helical heteropeptide (W1H5-21) and a 16-residue β-hairpin (GB41-56). Experimentally, we measured fluorescence energy transfer efficiency as a function of temperature, employing natural tryptophans as donors and dansylated lysines as acceptors. Secondary structural analysis was performed with circular dichroism and Fourier transform infrared spectroscopy.

Experiments and comprehensive simulations of the formation of a helical turn.

We investigate the kinetics and thermodynamics of a helical turn formation in the peptide Ac-WAAAH-NH(2). NMR measurements indicate that this peptide has significant tendency to form a structure of a helical turn, while temperature dependent CD establishes the helix fraction at different temperatures. Molecular dynamics and milestoning simulations agree with experimental observables and suggest an atomically detailed picture for the turn formation.

Unassisted transport of N-acetyl-L-tryptophanamide through membrane: experiment and simulation of kinetics.

Cellular transport machinery, such as channels and pumps, is working against the background of unassisted material transport through membranes. The permeation of a blocked tryptophan through a 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) membrane is investigated to probe unassisted or physical transport. The transport rate is measured experimentally and modeled computationally.

Structural dynamics of neuropeptide hPYY.

We have employed a combination of experiment and simulation to characterize the ensemble of structures sampled by human Peptide YY (hPYY), an important member of the neuropeptide Y family. Experimental structural characterization carried out with far UV circular dichroism spectroscopy and Fourier Transform-Infrared measurements confirmed that the major feature of the secondary structure of hPYY is the α-helix, encompassing about half the peptide residues, with smaller contributions from turn and β-sheet like structures. The peptide undergoes thermal denaturation characterized by a melting temperature of 48°C with an enthalpy change of -24.

Helix formation in a pentapeptide: experiment and force-field dependent dynamics.

We used a combined approach of experiment and simulation to determine the helical population and folding pathway of a small helix forming blocked pentapeptide, Ac-(Ala)(5)-NH(2). Experimental structural characterization of this blocked peptide was carried out with far UV circular dichroism spectroscopy, FTIR, and NMR measurements. These measurements confirm the presence of the α-helical state in a buffer solution.