Communicating without words: Measuring nonverbal communication between veterinarians and farmers during routine herd health consultations.

Uptake of advice and the ability to facilitate change on-farm are key elements for successful veterinary practice. However, having the necessary clinical skills and knowledge is not enough to achieve this: effective communication skills are essential for veterinarians to realize their advisory role by exploring and understanding the farmer's worldview. Research of verbal aspects of veterinarian communication supports the use of a relationship-centered communication style; we next need to study how veterinarian-farmer nonverbal communication (NVC) can influence interactions and their outcomes, which has been examined in medical and companion animal practice. In this study, we considered which aspects of NVC should be measured, and how, to provide an essential first step toward understanding the significance of NVC for veterinarians working in dairy practice, which should be of interest to researchers, veterinary educators, and practitioners. Eleven video recordings of routine consultations in the UK were analyzed for farmer and veterinarian NVC. The NVC attributes with established links to positive patient and client outcomes from medical and social science studies were chosen, and a methodology developed for their measurement, by adapting measures typically used in NVC research. Each consultation was segmented into intervals defined by the main activity and location on farm: introduction, fertility examination, discussion, and closing. This approach allowed us to analyze the content more consistently, establish which aspects of NVC featured within each interval, and whether the activity and location influenced the observed NVC. We measured 12 NVC attributes, including body orientation, interpersonal distance, head position, and body lean, which have been shown to influence empathy, rapport, and trust: key components of relationship-centered communication. Future research should seek to establish the significance of NVC in effective communication between veterinarian and farmer, building on our findings that show it is possible to measure nonverbal attributes. Veterinarians may benefit from becoming skilled nonverbal communicators and have more effective conversations during routine consultations, motivating farmers to make changes and improve herd health.

Alumni-based evaluation of a novel veterinary curriculum: are Nottingham graduates prepared for clinical practice?

INTRODUCTION: Outcomes-based education has been the core of the curriculum strategy of the Nottingham School of Veterinary Medicine and Science (SVMS) since its inception in 2006. As part of the ongoing curriculum evaluation, the first two graduating cohorts were invited to provide an appraisal of their preparation by the SVMS curriculum for their role in clinical practice. This paper provides brief accounts of the SVMS curriculum model, the development of the evaluation instrument and the findings of the alumni survey. MATERIALS AND METHODS: The evaluation instrument contained 25 attributes expected of SVMS graduates. Alumni rated their preparation for practice in relation to each attribute. RESULTS: The four highest rated characteristics were compassion for animals and the application of ethics to animal welfare; communication skills; recognising own limitations and seeking help and advice where needed and clinical examination skills. The four lowest rated were clinical case management and therapeutic strategies; dealing with veterinary public health and zoonotic issues; knowledge of current veterinary legislation and dealing with emergency and critical care cases. Free text responses were in line with these quantitative findings. CONCLUSION: The results indicate that this sample of SVMS graduates were satisfied with their undergraduate education and felt well prepared for their role in clinical practice.

Peptide mapping of complex proteins at the low-picomole level with capillary electrophoretic separations.

A variety of different peptide-mapping schemes are presented, with emphasis on the development of procedures which can be done with limited quantities (i.e. 5 pmol) of protein. Results are obtained from model proteins which contain disulfide bonds, which must be broken prior to fragmentation of the protein. A reaction involving the simultaneous use of tributylphosphine and 2-methylaziridine to reduce and alkylate the disulfide bonds is employed, due to favorable attributes of these reagents for the scaled-down procedure. The traditional performic acid oxidation reaction to cleave cystine groups is also successfully used with low-picomole quantities of protein. Three different protein digestion reagents are used: trypsin, chymotrypsin, and cyanogen bromide. Each reagent produces a unique mixture of peptides. Capillary electrophoresis is used to separate the peptides, offering high separation efficiencies, short analysis times, and compatibility with small sample sizes. In addition to the conventional use of UV detection for underivatized peptides, laser-induced fluorescence detection is employed in conjunction with an arginine-selective derivatization reaction. This latter procedure for derivatization and detection offers an alternative peptide-mapping mode, in which only the arginine-containing peptides are detected, and is useful in simplifying the peptide maps of large proteins.

Selective determination of arginine-containing and tyrosine-containing peptides using capillary electrophoresis and laser-induced fluorescence detection.

The use of two different amino acid-selective fluorogenic reagents for the derivatization of peptides is investigated. One such scheme utilizes a selective reaction of benzoin with the guanidine moiety to derivatize arginine residues occurring in a peptide. The second scheme involves the formylation of tyrosine, followed by reaction with 4-methoxy-1,2-phenylenediamine. The use of capillary electrophoresis and laser-induced fluorescence detection allows enhanced efficiencies and sensitivities to be obtained for the separations of either arginine- or tyrosine-containing peptides. A helium-cadmium laser (325 nm) is ideally suited for the laser-based detection system due to a close match of the excitation maxima of derivatized peptides from both reactions. A detection limit of 270 amol is achieved for model arginine-containing peptides, while the detection limit for model tyrosine-containing peptides is measured at 390 amol. Both derivatization reactions are found to be useful for high-sensitivity peptide mapping applications in which only the peptides containing the derivatized amino acids are detected.

Electrophoretic separations of proteins in capillaries with hydrolytically stable surface structures.

A procedure for obtaining highly stable coated capillaries for use in capillary electrophoresis (CE) is described. Reaction of surface-chlorinated fused silica capillaries with the Grignard reagent, vinyl magnesium bromide, followed by reaction of the vinyl group with acrylamide, results in an immobilized layer of polyacrylamide attached through hydrolytically stable Si-C bonds. This method is an extension of the capillary coating procedure described previously by Hjerten, differing in the means by which the polyacrylamide layer is bonded to the capillary walls. Capillaries treated in the manner described here can be used over a pH range of 2-10.5, without noticeable decomposition of the coating. In comparison to uncoated capillaries, separations of proteins using such coated capillaries are improved due to a reduction in protein adsorption to the capillary walls, although interaction is still present to some degree as evidenced by an inability to obtain plate counts as high as those predicted by theory. Electroosmotic flow is virtually eliminated in the coated capillaries, resulting in improved reproducibilities of protein migration times in comparison to uncoated capillaries. Additionally, peak skew is evaluated for model proteins and improvements are noted for the coated capillaries. Results are presented for separations of model protein mixtures, comparing the performance of the vinyl-bound polyacrylamide coated capillaries and uncoated capillaries at both high and low pH extremes.

Capillary electrophoretic separations of peptides using micelle-forming compounds and cyclodextrins as additives.

The value of electrokinetic capillary chromatography for separating structurally similar model peptides and tryptic digests is demonstrated. The behavior of model peptides in buffer systems containing dodecyltrimethylammonium bromide, hexadecyltrimethylammonium bromide, sodium dodecyl sulfate and two cyclodextrins as additives is described. These additives, under different analytical circumstances, exhibit certain beneficial effects for peptides with similar net charges but different hydrophobicities. Separations of underivatized peptides, utilizing UV detection, are presented. In addition, separation of fluorescent products of peptides derivatized with o-phthalaldehyde, fluorescamine, and a new reagent, 3-(4-carboxybenzoyl)-2-quinolinecarboxaldehyde, are demonstrated and discussed. Beneficial spectroscopic detection effects with cyclodextrin are also noted.

Recent advances in capillary electrophoresis of proteins, peptides and amino acids.

The current status of high-performance capillary electrophoresis as an analytical separation method for proteins, peptides and amino acids is assessed. Recent advances in suppressing the effects of electroosmotic flow and irreversible adsorption of proteins at the capillary wall are reviewed, together with procedures for optimal separations of peptides and amino acids. The detection aspects emphasize the role of laser-induced fluorescence and capillary electrophoresis/mass spectrometry in high-sensitivity measurements.

High-sensitivity peptide mapping by capillary zone electrophoresis and microcolumn liquid chromatography, using immobilized trypsin for protein digestion.

Procedures for the reduced-scale analysis of proteins by peptide mapping have been developed, allowing peptide maps to be obtained from picomole to femtomole quantities of protein. The use of trypsin immobilized on agarose gel and placed in a small reactor column has made it possible to reproducibility digest as little as 50 ng of protein. This represents a decrease in sample size of approximately 3 orders of magnitude from conventional tryptic digestion schemes. Separations of tryptic digests were accomplished by using either microcolumn high-performance liquid chromatography (HPLC) or capillary zone electrophoresis (CZE). Separations of 100 ng (4 pmol) of tryptic digest samples of beta-casein were achieved with microcolumn HPLC, while separations of approximately 2 ng (80 fmol) of beta-casein tryptic digest (from a total sample size of 50 ng) were possible with CZE. Peptide maps from phosphorylated and dephosphorylated forms of beta-casein were readily distinguishable using both separation methods, demonstrating an ability to detect a single amino acid modification in a protein. Relative standard deviations of peak retention or migration times were less than 3% for microcolumn HPLC and less than 1% for CZE.

Separation of precolumn ortho-phthalaldehyde-derivatized amino acids by capillary zone electrophoresis with normal and micellar solutions in the presence of organic modifiers.

Isoindole derivatives of amino acids, formed through a well-established reaction with o-phthalaldehyde, have been effectively resolved by capillary zone electrophoresis and detected fluorimetrically. Relative retention of the formed derivatives is strongly influenced by added detergents and organic modifiers. Analytical reproducibility has also been assessed.