Behind the doors of home hospice patients: A secondary qualitative analysis of hospice nurse communication with patients and families.

OBJECTIVE: Hospice nurses frequently encounter patients and families under tremendous emotional distress, yet the communication techniques they use in emotionally charged situations have rarely been investigated. In this study, researchers sought to examine hospice nurses' use of validation communication techniques, which have been shown in prior research to be effective in supporting individuals experiencing emotional distress. METHOD: Researchers performed a directed content analysis of audiorecordings of 65 hospice nurses' home visits by identifying instances when nurses used validation communication techniques and rating the level of complexity of those techniques. RESULT: All nurses used validation communication techniques at least once during their home visits. Use of lower level (i.e., more basic) techniques was more common than use of higher level (i.e., more complex) techniques. SIGNIFICANCE OF RESULTS: Although hospice nurses appear to use basic validation techniques naturally, benefit may be found in the use of higher level techniques, which have been shown to result in improved clinical outcomes in other settings.

Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.

This paper describes the role of α-subunit VISIT-DG sequence residue αThr-349 in the catalytic sites of Escherichia coli F1Fo ATP synthase. X-ray structures show the highly conserved αThr-349 in the proximity (2.68 Å) of the conserved phosphate binding residue ßR182 in the phosphate binding subdomain. αT349A, -D, -Q, and -R mutations caused 90-100-fold losses of oxidative phosphorylation and reduced ATPase activity of F1Fo in membranes. Double mutation αT349R/ßR182A was able to partially compensate for the absence of known phosphate binding residue ßR182. Azide, fluoroaluminate, and fluoroscandium caused insignificant inhibition of αT349A, -D, and -Q mutants, slight inhibition of the αT349R mutant, partial inhibition of the αT349R/ßR182A double mutant, and complete inhibition of the wild type. Whereas NBD-Cl (7-chloro-4-nitrobenzo-2-oxa-1,3-diazole) inhibited wild-type ATPase and its αT349A, -D, -R, and -Q mutants essentially completely, ßR182A ATPase and double mutant αT349A/ßR182A were inhibited partially. Inhibition characteristics supported the conclusion that NBD-Cl reacts in ßE (empty) catalytic sites, as shown previously by X-ray structure analysis. Phosphate protected against NBD-Cl inhibition in the wild type, αT349R, and double mutant αT349R/ßR182A but not in αT349A, αT349D, or αT349Q. The results demonstrate that αThr-349 is a supplementary residue involved in phosphate binding and transition state stabilization in ATP synthase catalytic sites through its interaction with ßR182.