General pediatric attending physicians' and residents' knowledge of inpatient hospital finances.

BACKGROUND AND OBJECTIVE: There is evidence suggesting that physicians have a limited foundation of knowledge on health care finances and limited awareness of hospital costs and charges. The objective was to analyze general pediatric attending physicians' and residents' knowledge of costs, charges, and reimbursements for care rendered in the inpatient setting. METHODS: An online survey was administered to all general pediatric attending physicians who work on the inpatient service and the entire pediatric residency program at The Children's Hospital of Philadelphia (CHOP) in spring of 2011. Participants' estimates of costs, charges, and reimbursements for several common tests, medications, and services were obtained and analyzed. RESULTS: A total of 38 attending physicians and 100 residents participated in the study (84% and 76% response rates, respectively). The majority of both attending physicians (71%) and residents (75%) characterized their understanding as "Minimally knowledgeable" or "Completely unaware". Only 15% of attending physicians' estimates and 11% of residents' estimates were within ±25% of true values across all surveyed costs, charges, and reimbursements. Percent error did not vary by level of experience or self-reported knowledge for attending physicians and residents. CONCLUSIONS: Attending physicians and residents demonstrated limited knowledge of costs, charges, and reimbursements as shown by a low accuracy of estimates and a high percent error, compared with the actual values. To meet expectations for competency in systems-based practice and to be effective stewards of medical resources, it appears that pediatricians need further financial education.

The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain.

The KRAB domain is a 75 amino acid transcriptional repression module that is encoded by more than 400 zinc finger protein genes, making it the most abundant repression domain in the human proteome. KRAB-mediated gene silencing requires a direct high affinity interaction with the RBCC domain of KAP-1 co-repressor. The structures of the free KRAB domain or the KRAB-RBCC complex are unknown. To address this, we have performed a systematic biophysical analysis of all KRAB isoforms using purified recombinant proteins. All KRAB domains are predominantly monomeric either alone or in a complex with KAP-1-RBCC protein, while a KRAB-SCAN isoform exists as a stable dimer. The KRAB:KAP-1-RBCC interaction requires only the A box in the context of the KRAB(Ab) or KRAB(AC) but both A and B boxes in the context of KRAB(AB). All isoforms bind the KAP-1-RBCC in a stable, zinc dependent fashion with a stoichiometry of KRAB1:3 RBCC with a zinc content of four atoms per RBCC monomer. Limited proteolysis, mass spectrometry and N-terminal sequence analyses suggest that a core complex comprises the entire RBCC domain of KAP-1 and the AB box of the KRAB domain rendering it resistant to proteolysis. NMR spectroscopy showed that unbound KRAB domain does not exist as a well-folded globular protein in solution but may fold into an ordered structure upon binding to the KAP-1-RBCC protein. This is the first example of a structurally disordered repressor domain that is the most widely conserved silencing domain in tetrapods.