Perspectives of female physicians practicing in rural Wisconsin.

BACKGROUND: While approximately 30% of the Wisconsin population lives in rural areas, only 11% of physicians practice in these areas. More women are entering medicine today and some studies have raised concerns that women are less likely to practice in rural areas. The intent of this study was to identify which factors influenced female physicians to enter rural practice and to look at the issues they are confronting. METHODS: Ten female physicians practicing in rural Wisconsin towns agreed to participate in 30- to 60-minute semi-structured interviews. Transcripts of the interviews were analyzed to identify common themes in answers to the questions. RESULTS: The physicians had been in practice between 2-26 years, with an average of 13 years. Seven of the 10 had rural backgrounds, which influenced their decisions to practice in rural areas. The physicians cited other factors, such as professional satisfaction, the ability to be engaged with and serve one's community, and having a good place to raise one's family, that made practicing and living in a rural community attractive. However, these physicians also found some drawbacks to rural practice, including too few providers, too much call, and finding a balance between professional and family life. Despite this, all plan to stay in their current practices indefinitely and recommend rural practice to female medical students and residents. CONCLUSIONS: These female physicians find the value of being in rural practice overcome the challenges. The participants provided insight into motivating women to enter rural practice, finding a balance between the challenges and benefits of rural medicine, and promoting the future of rural health care.

Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices.

Very little is known about how protein structure evolves during the polypeptide chain elongation that accompanies cotranslational protein folding. This in vitro model study is aimed at probing how conformational space evolves for purified N-terminal polypeptides of increasing length. These peptides are derived from the sequence of an all-alpha-helical single domain protein, Sperm whale apomyoglobin (apoMb). Even at short chain lengths, ordered structure is found. The nature of this structure is strongly chain length dependent. At relatively short lengths, a predominantly non-native beta-sheet conformation is present, and self-associated amyloid-like species are generated. As chain length increases, alpha-helix progressively takes over, and it replaces the beta-strand. The observed trends correlate with the specific fraction of solvent-accessible nonpolar surface area present at different chain lengths. The C-terminal portion of the chain plays an important role by promoting a large and cooperative overall increase in helical content and by consolidating the monomeric association state of the full-length protein. Thus, a native-like energy landscape develops late during apoMb chain elongation. This effect may provide an important driving force for chain expulsion from the ribosome and promote nearly-posttranslational folding of single domain proteins in the cell. Nature has been able to overcome the above intrinsic misfolding trends by modulating the composition of the intracellular environment. An imbalance or improper functioning by the above modulating factors during translation may play a role in misfolding-driven intracellular disorders.