Targeting schema change in social anxiety via autobiographical memory reconstruction.

Negative self-schemas are fundamental to social anxiety disorder and contribute to its persistence, thus understanding how to change schemas is of critical importance. Memory-based interventions and associated theories propose that reconstructing autobiographical memories tethered to schemas with conceptual details that challenge the associated expectations will lead to schema change. Here, we test this proposal in a between-subjects behavioural experiment with undergraduate participants with social anxiety.

The Neural Corelates of Constructing Conceptual and Perceptual Representations of Autobiographical Memories.

Contemporary neurocognitive frameworks propose that conceptual and perceptual content of autobiographical memories-personal past experiences-are processed by dissociable neural systems. Other work has proposed a central role of the anterior hippocampus in initially constructing autobiographical memories, regardless of the content. Here, we report on an fMRI study that utilized a repeated retrieval paradigm to test these ideas.

Molecular Dynamics Simulations of 441 Two-Residue Peptides in Aqueous Solution: Conformational Preferences and Neighboring Residue Effects with the Amber ff99SB-ildn-NMR Force Field.

Understanding the intrinsic conformational preferences of amino acids and the extent to which they are modulated by neighboring residues is a key issue for developing predictive models of protein folding and stability. Here we present the results of 441 independent explicit-solvent MD simulations of all possible two-residue peptides that contain the 20 standard amino acids with histidine modeled in both its neutral and protonated states. (3)J(HNHα) coupling constants and δ(Hα) chemical shifts calculated from the MD simulations correlate quite well with recently published experimental measurements for a corresponding set of two-residue peptides.

Parametrization of Backbone Flexibility in a Coarse-Grained Force Field for Proteins (COFFDROP) Derived from All-Atom Explicit-Solvent Molecular Dynamics Simulations of All Possible Two-Residue Peptides.

Recently, we reported the parametrization of a set of coarse-grained (CG) nonbonded potential functions, derived from all-atom explicit-solvent molecular dynamics (MD) simulations of amino acid pairs and designed for use in (implicit-solvent) Brownian dynamics (BD) simulations of proteins; this force field was named COFFDROP (COarse-grained Force Field for Dynamic Representations Of Proteins). Here, we describe the extension of COFFDROP to include bonded backbone terms derived from fitting to results of explicit-solvent MD simulations of all possible two-residue peptides containing the 20 standard amino acids, with histidine modeled in both its protonated and neutral forms. The iterative Boltzmann inversion (IBI) method was used to optimize new CG potential functions for backbone-related terms by attempting to reproduce angle, dihedral, and distance probability distributions generated by the MD simulations.