Attentional capture by salient distractors during visual search is determined by temporal task demands.

The question whether attentional capture by salient but task-irrelevant visual stimuli is triggered in a bottom-up fashion or depends on top-down task settings is still unresolved. Strong support for bottom-up capture was obtained in the additional singleton task, in which search arrays were visible until response onset. Equally strong evidence for top-down control of attentional capture was obtained in spatial cueing experiments in which display durations were very brief.

Précis of bayesian rationality: The probabilistic approach to human reasoning.

According to Aristotle, humans are the rational animal. The borderline between rationality and irrationality is fundamental to many aspects of human life including the law, mental health, and language interpretation. But what is it to be rational? One answer, deeply embedded in the Western intellectual tradition since ancient Greece, is that rationality concerns reasoning according to the rules of logic--the formal theory that specifies the inferential connections that hold with certainty between propositions.

Reward priority of visual target singletons modulates event-related potential signatures of attentional selection.

We examined visual search for color singleton targets, whose shape was discriminated. Critically, we varied the reward priority of singleton colors (correct fast performance was worth more bonus points for red singletons than for green singletons, or vice versa) to test whether event-related potential signatures of visual selection can be affected by distinct reward priorities for different target types, even when every target has to be selected for report. The N2pc component was earlier and larger for high- than for low-reward targets.

Expression, reconstitution, and structure of an archaeal RNA degrading exosome.

The exosome is a protein complex that participates in a wide variety of RNA processing, degradation, and quality-control pathways. The exosome is conserved in all eukaryotes studied to date and is also present in many archaeal organisms, albeit in a simpler form. To gain insights into the architecture of the exosome complex, we have chosen the hyperthermophilic archaeum Sulfolobus solfataricus as a model system.

Structural organization of the RNA-degrading exosome.

The RNA exosome participates in the degradation and processing of a wide range of RNA molecules. Recent advances in understanding how the exosome is organized and functions largely stem from structural studies. Crystal structures of archaeal exosomes bound to RNA and of the corresponding nine-subunit human exosome core show that the archaeal and eukaryotic complexes have a similar molecular architecture, but have a diverged catalytic mechanism.

Adaptive non-interventional heuristics for covariation detection in causal induction: model comparison and rational analysis.

In this article, 41 models of covariation detection from 2 × 2 contingency tables were evaluated against past data in the literature and against data from new experiments. A new model was also included based on a limiting case of the normative phi-coefficient under an extreme rarity assumption, which has been shown to be an important factor in covariation detection (McKenzie & Mikkelsen, 2007) and data selection (Hattori, 2002; Oaksford & Chater, 1994, 2003). The results were supportive of the new model.

Topologies of a substrate protein bound to the chaperonin GroEL.

The chaperonin GroEL assists polypeptide folding through sequential steps of binding nonnative protein in the central cavity of an open ring, via hydrophobic surfaces of its apical domains, followed by encapsulation in a hydrophilic cavity. To examine the binding state, we have classified a large data set of GroEL binary complexes with nonnative malate dehydrogenase (MDH), imaged by cryo-electron microscopy, to sort them into homogeneous subsets. The resulting electron density maps show MDH associated in several characteristic binding topologies either deep inside the cavity or at its inlet, contacting three to four consecutive GroEL apical domains.

Interatomic potential models for natural apatite crystals: incorporating strontium and the lanthanides.

A comprehensive set of interatomic potential parameters for modeling natural apatite crystals is presented. These potentials build on those previously used in research on apatites with new potentials fitted empirically to crystal structures and their properties using the GULP program. We demonstrate that the new potentials produce good models for the different compounds used for fitting, as well as for several natural apatites.

A universally applicable method of operon map prediction on minimally annotated genomes using conserved genomic context.

An important step in understanding the regulation of a prokaryotic genome is the generation of its transcription unit map. The current strongest operon predictor depends on the distributions of intergenic distances (IGD) separating adjacent genes within and between operons. Unfortunately, experimental data on these distance distributions are limited to Escherichia coli and Bacillus subtilis.

Challenges at the frontiers of structural biology.

A recent meeting brought together electron microscopists, crystallographers and modellers to consider the problems facing structural biologists who wish to understand large, subcellular machines, and how the methods should be extended to achieve this goal.

ATP-bound states of GroEL captured by cryo-electron microscopy.

The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously discharging the previous folding chamber from the opposite ring. The GroEL-ATP structure, determined by cryo-EM and atomic structure fitting, shows that the intermediate domains rotate downward, switching their intersubunit salt bridge contacts from substrate binding to ATP binding domains. These observations, together with the effects of ATP binding to a GroEL-GroES-ADP complex, suggest structural models for the ATP-induced reduction in affinity for polypeptide and for cooperativity.

Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy.

We have developed an angular refinement procedure incorporating correction for the microscope contrast transfer function, to determine cryoelectron microscopy (cryo-EM) structures of the Escherichia coli chaperonin GroEL in its apo and ATP-bound forms. This image reconstruction procedure is verified to 13-A resolution by comparison of the cryo-EM structure of unliganded GroEL with the crystal structure. Binding, encapsulation, and release of nonnative proteins by GroEL and its cochaperone GroES are controlled by the binding and hydrolysis of ATP.

Chaperonins.

The molecular chaperones are a diverse set of protein families required for the correct folding, transport and degradation of other proteins in vivo. There has been great progress in understanding the structure and mechanism of action of the chaperonin family, exemplified by Escherichia coli GroEL. The chaperonins are large, double-ring oligomeric proteins that act as containers for the folding of other protein subunits.

What can electron microscopy tell us about chaperoned protein folding?

Chaperonins form large, cage-like structures that act as protein folding machines. Recent developments in electron cryo-microscopy and image processing are helping to reveal the mechanism of chaperonin-mediated protein folding.

Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

Protein folding mediated by the molecular chaperone GroEL occurs by its binding to non-native polypeptide substrates and is driven by ATP hydrolysis. Both of these processes are influenced by the reversible association of the co-protein, GroES (refs 2-4). GroEL and other chaperonin 60 molecules are large, cylindrical oligomers consisting of two stacked heptameric rings of subunits; each ring forms a cage-like structure thought to bind polypeptides in a central cavity.

Proton NMR studies of bovine serum albumin. Assignment of spin systems.

A variety of one- and two-dimensional 1H-NMR methods have been applied to the study of defatted 66.5-kDa bovine serum albumin in solution. 1.

Helix geometry in proteins.

In this report we describe a general survey of all helices found in 57 of the known protein crystal structures, together with a detailed analysis of 48 alpha-helices found in 16 of the structures that are determined to high resolution. The survey of all helices reveals a total of 291 alpha-helices, 71 3(10)-helices and no examples of pi-helices. The conformations of the observed helices are significantly different from the "ideal" linear structures.