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Background: The Patient Protection and Affordable Care Act of 2010 includes patient satisfaction scores in the calculation of reimbursement for services provided. The Medicare and Medicaid Electronic Health Care Record Incentive Program mandate that physicians provide electronic communication with patients. Little data exists regarding patient preferences that might guide the physician adhering to these guidelines. We performed a survey study to examine patients' attitudes regarding the delivery of their health care., Methods: We provided an anonymous survey to all outpatient hand surgery patients within a 1-month period at our level I academic center. The survey was structured to ascertain patients' attitudes toward outpatient wait times as well as delivery of patient-specific healthcare-related information. One-hundred and ninety-six surveys were available for review., Results: Of the 196 patients surveyed, 106 (54 %) were between the ages of 45 and 64. Patients aged 25 to 44 were the least willing to wait for an initial outpatient appointment. The majority of patients in all age groups demonstrated unwillingness to wait more than 1 week for evaluation of a new problem. One hundred and forty patients (71 %) were willing to wait longer for an appointment with an upper extremity specialist rather than have an earlier appointment with a non-upper extremity specialist. Wait times of 30 min after arrival in the office were acceptable to 174 patients (89 %) while 40 patients (20 %) were willing to wait an hour or more. Patients preferred a typed handout detailing their specific problem as opposed to referral to a website or an e-mail containing information., Conclusions: The results of our study indicate that patients prefer typed information as opposed to e-mail or websites regarding their health care. Our study also suggests that patients are willing to endure longer wait times if they can be given a sooner appointment, and most prefer a specialist for their problems. These results will provide some guidance to the physician regarding what patients find most appealing.

Fluorescent probe pairs that can be selectively excited in the presence of Trp and Tyr are of great utility in studying conformational changes in proteins. However, the size of these probe pairs can restrict their incorporation to small portions of a protein sequence where their effects on secondary and tertiary structure can be tolerated. Our findings show that a thioamide bond-a single atom substitution of the peptide backbone-can quench fluorophores that are red-shifted from intrinsic protein fluorescence, such as acridone. Using steady-state and fluorescence lifetime measurements, we further demonstrate that this quenching occurs through a dynamic electron-transfer mechanism. In a proof-of-principle experiment, we apply this technique to monitor unfolding in a model peptide system, the villin headpiece HP35 fragment. Thioamide analogues of the natural amino acids can be placed in a variety of locations in a protein sequence, allowing one to make a large number of measurements to model protein folding., (© 2012 American Chemical Society)

Methods for synthetically manipulating protein structure enable greater flexibility in the study of protein function. Previous characterization of the Escherichia coli aminoacyl tRNA transferase (AaT) has shown that it can modify the N-terminus of a protein with an amino acid from a tRNA or a synthetic oligonucleotide donor. Here, we demonstrate that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials. We have characterized the enzymatic activity of AaT with aminoacyl adenosyl donors and found that reaction products do not inhibit AaT. The use of adenosyl donors removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor. Thus, our AaT donors increase the potential substrate scope and reaction scale for N-terminal protein modification under conditions that maintain folding.