Publications by authors named "H B Tepper"

Shape and weight overvaluation is a core component of body image theorized to drive many of the symptoms of eating disorders (ED) and associated distress and impairment. Identifying variables that protect against the negative effects of shape and weight overvaluation is needed for informing primary intervention targets. Self-compassion may be a protective factor given its role as an adaptive affect regulation strategy.

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Objective: E-therapy shows promise as a solution to the barriers that stand in the way of people receiving eating disorder (ED) treatment. Despite the potential for e-therapy to reduce the well-known treatment gap, little is known about public views and perspectives on this mode of intervention delivery. This study explored attitudes toward, and preferences for, e-therapy among individuals spanning the spectrum of eating pathology.

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This experiment examined asymmetries in the execution of an object manipulation task that requires the coordinated use of both hands. To this end, twenty right-hand-dominant participants performed a bimanual object manipulation task, which required that they reach for and grasp two objects located on a tabletop, fit the two objects through a hole in a horizontally or vertically oriented fitting board, and then rotate the objects 180° to produce a "beep" tone. Overall, the two hands were highly synchronized at the start, but not at end, of each movement phase.

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How chaperone interactions affect protein folding pathways is a central problem in biology. With the use of optical tweezers and all-atom molecular dynamics simulations, we studied the effect of chaperone SecB on the folding and unfolding pathways of maltose binding protein (MBP) at the single-molecule level. In the absence of SecB, we find that the MBP polypeptide first collapses into a molten globulelike compacted state and then folds into a stable core structure onto which several alpha helices are finally wrapped.

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Multistate empirical valence bond simulations were employed to study proton transport through gramicidin A channels embedded in two different lipid bilayers, glycerol 1-monooleate (GMO) and diphytanolphosphatidylcholine (DiPhPC). Free energy barriers to proton permeation were derived using a new internal reaction coordinate describing the proton permeation process. The large quantitative and qualitative differences between the two systems are discussed in terms of local bilayer structures, ordering of interfacial water, and channel flexibility in the two environments.

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