RESUMEN
OBJECTIVE: To investigate the relationship between a micropulse vibration device and pain perception during orthodontic treatment. MATERIALS AND METHODS: This study was a parallel group, randomized clinical trial. A total of 58 patients meeting eligibility criteria were assigned using block allocation to one of two groups: an experimental group using the vibration device or a control group (n â=â 29 for each group). Patients used the device for 20 minutes daily. Patients rated pain intensity on a visual analog scale at appropriate intervals during the weeks after the separator or archwire appointment. Data were analyzed using repeated measures analysis of variance at α â=â .05. RESULTS: During the 4-month test period, significant differences between the micropulse vibration device group and the control group for overall pain (P â=â .002) and biting pain (P â=â .003) were identified. The authors observed that perceived pain was highest at the beginning of the month, following archwire adjustment. CONCLUSION: The micropulse vibration device significantly lowered the pain scores for overall pain and biting pain during the 4-month study period.
Asunto(s)
Ortodoncia , Manejo del Dolor , Vibración , Adolescente , Adulto , Niño , Femenino , Humanos , Masculino , Dolor , Dimensión del Dolor , Adulto JovenRESUMEN
High-resolution structural information is important for improving our understanding of protein function in vitro and in vivo and providing information to enable drug discovery. The process leading to X-ray structure determination is often time consuming and labor intensive. It requires informed decisions in expression construct design, expression host selection, and strategies for protein purification, crystallization and structure determination. Previously published studies have demonstrated that compact globular domains defined by limited proteolysis represent good candidates for production of diffraction quality crystals [1-7]. Integration of mass spectrometry and proteolysis experiments can provide accurate definition of domain boundaries at unprecedented rates. We have conducted a critical evaluation of this approach with 400 target proteins produced by SGX (Structural GenomiX, Inc.) for the New York Structural GenomiX Research Consortium (NYSGXRC; http://www.nysgxrc.org) under the auspices of the National Institute of General Medical Sciences Protein Structure Initiative (http://www.nigms.nih.gov/psi). The objectives of this study were to develop parallel/automated protocols for proteolytic digestion and data acquisition for multiple proteins, and to carry out a systematic study to correlate domain definition via proteolysis with outcomes of crystallization and structure determination attempts. Initial results from this work demonstrate that proteins yielding diffraction quality crystals are typically resistant to proteolysis. Large-scale sub cloning and subsequent testing of expression, solubility, and crystallizability of proteolytically defined truncations is currently underway.