Publications by authors named "Robert Boyko"

Background: Caring for loved ones with palliative needs can be very stressful for carers'. To address this growing issue, an online Home Caregiver Support Program course was created to provide information to non-professional home caregivers about end-of-life care.

Objectives: To measure non-professional caregivers' perceived level of competence in addressing physical, psychological, social, and spiritual needs before and after completing online training modules.

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Introduction: We conducted an overview of systematic reviews of interventions for the prevention of low back pain (LBP) that can be conducted in a workplace setting.

Methods: An electronic literature search was performed in Medline, EMBASE, and the Cochrane Library. Published peer-reviewed systematic reviews and meta-analyses, which described interventions for the primary or secondary prevention of LBP applicable to a workplace setting, were eligible for inclusion.

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Laboratories often repeatedly determine the structure of a given protein under a variety of conditions, mutations, modifications, or in a number of states. This approach can be cumbersome and tedious. Given then a database of structures, identifiers, and corresponding (1)H,(15)N-HSQC NMR spectra for homologous proteins, we investigated whether structural information could be ascertained for a new homolog solely from its (1)H,(15)N-HSQC NMR spectrum.

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We have addressed the electrostatic interactions occurring between the inhibitory region of cardiac troponin I with the C-lobe of troponin C using scanning glycine mutagenesis of the inhibitory region. We report variations in the electric potentials due to mutation of charged residues within this complex based upon the solved NMR structure (1OZS). These results demonstrate the importance of electrostatics within this complex, and it is proposed that electrostatic interactions are integral to the formation and function of larger ternary troponin complexes.

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Complete and accurate NMR spectral assignment is a prerequisite for high-throughput automated structure determination of biological macromolecules. However, completely automated assignment procedures generally encounter difficulties for all but the most ideal data sets. Sources of these problems include difficulty in resolving correlations in crowded spectral regions, as well as complications arising from dynamics, such as weak or missing peaks, or atoms exhibiting more than one peak due to exchange phenomena.

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VADAR (Volume Area Dihedral Angle Reporter) is a comprehensive web server for quantitative protein structure evaluation. It accepts Protein Data Bank (PDB) formatted files or PDB accession numbers as input and calculates, identifies, graphs, reports and/or evaluates a large number (>30) of key structural parameters both for individual residues and for the entire protein. These include excluded volume, accessible surface area, backbone and side chain dihedral angles, secondary structure, hydrogen bonding partners, hydrogen bond energies, steric quality, solvation free energy as well as local and overall fold quality.

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A new simulation program for multinuclear NMR is introduced. PJNMR (Pure Java NMR) 2.0, written entirely in the Java programming language, simulates pulse sequences on systems of up to three weakly coupled spins-1/2 with a command-driven, spectrometer-like interface.

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