Belief Change and Memory for Previous Beliefs after Comprehension of Contentious Scientific Information

We explored the relationship between belief change and recollection of previous beliefs. Subjects reported beliefs about TV violence. Later, subjects read a one-sided, belief inconsistent text. We manipulated whether subjects reported beliefs after reading first, or recollected previous beliefs first. A third group was told their previous beliefs before reporting current beliefs. Recollections were not improved when subjects recollected beliefs first. When told previous beliefs, belief change was reduced, suggesting a desire to appear consistent

The impact of the Self-Determined Learning Model of Instruction on student self-determination

This is the publisher's version, also found here: http://cec.metapress.com/content/c5n78j60w945vk2x/?p=9b7820f03e7c4a37be218efe08d17483&pi=0Promoting self-determination has become a best practice in special education. There remains, however, a paucity of causal evidence for interventions to promote self-determination. This article presents the results of a group-randomized, modified equivalent control group design study of the efficacy of the Self Determined Learning Model of Instruction (SDLMI, Wehmeyer, Palmer, Agran, Mithaug, & Martin, 2000) to promote self-determination. The authors used data on self-determination using multiple measures collected with 312 high school students with cognitive disabilities in both a control and a treatment group to examine the relationship between the SDLMI and self-determination. After determining strong measurement invariance for each latent construct, they found significant differences in latent means across measurement occasions and differential effects attributable to the SDLMI. This was true across disability category, though there was variance across disability populations

The Structure of β-Carbonic Anhydrase from the Carboxysomal Shell Reveals a Distinct Subclass with One Active Site for the Price of Two

CsoSCA (formerly CsoS3) is a bacterial carbonic anhydrase localized in the shell of a cellular microcompartment called the carboxysome, where it converts HCO-3 to CO2 for use in carbon fixation by ribulose-bisphosphate carboxylase/oxygenase (RuBisCO). CsoSCA lacks significant sequence similarity to any of the four known classes of carbonic anhydrase (α, β, γ, or δ), and so it was initially classified as belonging to a new class, ϵ. The crystal structure of CsoSCA from Halothiobacillus neapolitanus reveals that it is actually a representative member of a new subclass of β-carbonic anhydrases, distinguished by a lack of active site pairing. Whereas a typical β-carbonic anhydrase maintains a pair of active sites organized within a two-fold symmetric homodimer or pair of fused, homologous domains, the two domains in CsoSCA have diverged to the point that only one domain in the pair retains a viable active site. We suggest that this defunct and somewhat diminished domain has evolved a new function, specific to its carboxysomal environment. Despite the level of sequence divergence that separates CsoSCA from the other two subclasses of β-carbonic anhydrases, there is a remarkable level of structural similarity among active site regions, which suggests a common catalytic mechanism for the interconversion of HCO-3 and CO2. Crystal packing analysis suggests that CsoSCA exists within the carboxysome shell either as a homodimer or as extended filaments

Structural Analysis of CsoS1A and the Protein Shell of the \u3ci\u3eHalothiobacillus neapolitanus\u3c/i\u3e Carboxysome

The carboxysome is a bacterial organelle that functions to enhance the efficiency of CO2 fixation by encapsulating the enzymes ribulose bisphosphate carboxylase/ oxygenase (RuBisCO) and carbonic anhydrase. The outer shell of the carboxysome is reminiscent of a viral capsid, being constructed from many copies of a few small proteins. Here we describe the structure of the shell protein CsoS1A from the chemoautotrophic bacterium Halothiobacillus neapolitanus. The CsoS1A protein forms hexameric units that pack tightly together to form a molecular layer, which is perforated by narrow pores. Sulfate ions, soaked into crystals of CsoS1A, are observed in the pores of the molecular layer, supporting the idea that the pores could be the conduit for negatively charged metabolites such as bicarbonate, which must cross the shell. The problem of diffusion across a semiporous protein shell is discussed, with the conclusion that the shell is sufficiently porous to allow adequate transport of small molecules. The molecular layer formed by CsoS1A is similar to the recently observed layers formed by cyanobacterial carboxysome shell proteins. This similarity supports the argument that the layers observed represent the natural structure of the facets of the carboxysome shell. Insights into carboxysome function are provided by comparisons of the carboxysome shell to viral capsids, and a comparison of its pores to the pores of transmembrane protein channels

Random Walks for Spike-Timing Dependent Plasticity

Random walk methods are used to calculate the moments of negative image equilibrium distributions in synaptic weight dynamics governed by spike-timing dependent plasticity (STDP). The neural architecture of the model is based on the electrosensory lateral line lobe (ELL) of mormyrid electric fish, which forms a negative image of the reafferent signal from the fish's own electric discharge to optimize detection of sensory electric fields. Of particular behavioral importance to the fish is the variance of the equilibrium postsynaptic potential in the presence of noise, which is determined by the variance of the equilibrium weight distribution. Recurrence relations are derived for the moments of the equilibrium weight distribution, for arbitrary postsynaptic potential functions and arbitrary learning rules. For the case of homogeneous network parameters, explicit closed form solutions are developed for the covariances of the synaptic weight and postsynaptic potential distributions.Comment: 18 pages, 8 figures, 15 subfigures; uses revtex4, subfigure, amsmat

Structural basis for activation of calcineurin by calmodulin

The highly conserved phosphatase calcineurin plays vital roles in numerous processes including T-cell activation, development and function of the central nervous system, and cardiac growth. It is activated by the calcium sensor calmodulin. Calmodulin binds to a regulatory domain within calcineurin, causing a conformational change that displaces an autoinhibitory domain from the active site, resulting in activation of the phosphatase. This is the same general mechanism by which calmodulin activates calmodulin-dependent protein kinases. Previously published data has hinted that the regulatory domain of calcineurin is intrinsically disordered. In this work we demonstrate that the regulatory domain is unstructured and that it folds upon binding calmodulin, ousting the autoinhibitory domain from the catalytic site. The regulatory domain is 95 residues long, with the autoinhibitory domain attached to its C-terminal end and the 24 residue calmodulin binding region towards the N-terminal end. This is unlike the calmodulin-dependent protein kinases which have calmodulin binding sites and autoinhibitory domains immediately adjacent in sequence. Our data demonstrate that not only does the calmodulin binding region fold, but that an ~25-30 residue region between it and the autoinhibitory domain also folds, resulting in over half of the regulatory domain adopting α-helical structure. This appears to be the first observation of calmodulin inducing folding of this scale outside of its binding site on a target protein

Structural Basis for Activation of Calcineurin by Calmodulin

The highly conserved phosphatase calcineurin (CaN) plays vital roles in numerous processes including T-cell activation, development and function of the central nervous system, and cardiac growth. It is activated by the calcium sensor calmodulin (CaM). CaM binds to a regulatory domain (RD) within CaN, causing a conformational change that displaces an autoinhibitory domain (AID) from the active site, resulting in activation of the phosphatase. This is the same general mechanism by which CaM activates CaM-dependent protein kinases. Previously published data have hinted that the RD of CaN is intrinsically disordered. In this work, we demonstrate that the RD is unstructured and that it folds upon binding CaM, ousting the AID from the catalytic site. The RD is 95 residues long, with the AID attached to its C-terminal end and the 24-residue CaM binding region toward the N-terminal end. This is unlike the CaM-dependent protein kinases that have CaM binding sites and AIDs immediately adjacent in sequence. Our data demonstrate that not only does the CaM binding region folds but also an ∼25- to 30-residue region between it and the AID folds, resulting in over half of the RD adopting α-helical structure. This appears to be the first observation of CaM inducing folding of this scale outside of its binding site on a target protein

20th to 21st Century Relative Sea and Land Level Changes in Northern California: Tectonic Land Level Changes and their Contribution to Sea-Level Rise, Humboldt Bay Region, Northern California

Sea-level changes are modulated in coastal northern California by land-level changes due to the earthquake cycle along the Cascadia subduction zone, the San Andreas plate boundary fault system, and crustal faults. Sea-level rise (SLR) subjects ecological and anthropogenic infrastructure to increased vulnerability to changes in habitat and increased risk for physical damage. The degree to which each of these forcing factors drives this modulation is poorly resolved. We use NOAA tide gage data and ‘campaign’ tide gage deployments, Global Navigation Satellite System (GNSS) data, and National Geodetic Survey (NGS) first-order levelling data to calculate vertical land motion (VLM) rates in coastal northern California. Sea-level observations, highway level surveys, and GNSS data all confirm that land is subsiding in Humboldt Bay, in contrast to Crescent City where the land is rising. Subtracting absolute sea-level rate (~1.99 mm/year) from Crescent City (CC) and North Spit (NS) gage relative sea-level rates reveals that CC is uplifting at ~2.83 mm/year and NS is subsiding at ~3.21mm/year. GNSS vertical deformation reveals similar rates of ~2.60 mm/year of uplift at Crescent City. In coastal northern California, there is an E-W trending variation in vertical land motion that is primarily due to Cascadia megathrust fault seismogenic coupling. This interseismic subsidence also dominates the N-S variation in vertical land motion in most of the study region. There exists a second-order heterogeneous N-S trend in vertical land motion that we associate to crustal fault-related strain. There may be non-tectonic contributions to the observed VLM rates