ABSTRACT
BACKGROUND: The present study aimed to explore facilitators and barriers to weight loss (WL) and weight loss maintenance (WLM) in women who participated in a primary, 18-week comparative trial that promoted WL with an energy-restricted diet. METHODS: Twenty-three women participated in seven focus groups conducted by a moderator and co-facilitator using open-ended questions and probes. Focus groups were held in a private room and audio tape-recorded. Tapes were transcribed verbatim and thematic analysis was used to evaluate transcripts for common themes. RESULTS: Accountability to others, social support, planning ahead, awareness and mindfulness of food choices, basic nutrition education, portion control, exercise, and self-motivation were perceived as key facilitators for WL and WLM by women. Identified barriers included life transitions, health status changes, internal factors, environmental pressures, lack of accountability and an absence of social support. CONCLUSIONS: Future interventions should address these salient facilitators and barriers to promote sustainable changes in women across their WL and WLM journeys.
Subject(s)
Caloric Restriction/psychology , Exercise/psychology , Food Preferences/psychology , Motivation/physiology , Qualitative Research , Weight Loss/physiology , Adult , Choice Behavior , Exercise/physiology , Female , Focus Groups , Food Preferences/physiology , Health Status , Humans , Social SupportABSTRACT
The Boredetella pertussis wlbD gene product is a putative uridine-5-diphosphate N-acetylglucosamine (UDP-GlcNAc) 2'-epimerase involved in Band A lipopolysaccharide biosynthesis. The wlbD gene is homologous to Escherichia coli rffE (32% identical), an established UDP-GlcNAc 2'-epimerase that is involved in enterobacterial common antigen (ECA) formation. The structure of the rffE protein reveals an unexpected role for a bound sodium ion in orientating a substrate-binding alpha-helix in the enzyme active site. Whilst key active-site residues in rffE are present in the wlbD sequence, the sodium-binding residues outside the active site are absent. This raises questions about the modulation of enzyme activity in these two enzymes. The wlbD gene from B. pertussis has been cloned and overexpressed in E. coli and the resulting protein has been purified to homogeneity. In the current study, crystals of the mutant Gln339Arg wlbD enzyme have been obtained by sitting-drop vapour diffusion. Uncomplexed Gln339Arg and UDP-GlcNAc complex data sets have been collected in-house on a rotating-anode generator to 2.1 A. Combined, the data sets identify the space group as P2(1)2(1)2(1), with unit-cell parameters a = 78, b = 91, c = 125 A, alpha = beta = gamma = 90 degrees. The asymmetric unit contains two monomers and 53% solvent.
