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The commentaries raise a host of challenging issues and reflect a broad range of views. Some commentators doubt that there is any convincing evidence for adaptive misbelief, and remain (in our view, unduly) wedded to our 'default presumption' that misbelief is maladaptive. Others think that the evidence for adaptive misbelief is so obvious, and so widespread, that the label 'default presumption' is disingenuous. We try to chart a careful course between these opposing perspectives. doi:10.1017/S0140525X09991555

From an evolutionary standpoint, a default presumption is that true beliefs are adaptive and misbeliefs maladaptive. But if humans are biologically engineered to appraise the world accurately and to form true beliefs, how are we to explain the routine exceptions to this rule? How can we account for mistaken beliefs, bizarre delusions, and instances, of self-deception? We explore this question in some detail. We begin by articulating a distinction between two general types of misbelief: those resulting from a breakdown in the normal functioning of the belief formation system (e.g., delusions) and those arising in the normal course of that system's operations (e.g., beliefs based on incomplete or inaccurate information). The former are instances of biological dysfunction or pathology, reflecting 'culpable' limitations of evolutionary design. Although the latter category includes undesirable (but tolerable) by-products of 'forgivably' limited design, our quarry is a contentious subclass of this category: misbeliefs best conceived as design features. Such misbeliefs, unlike occasional lucky falsehoods, would have been systematically adaptive in the evolutionary past. Such misbeliefs, furthermore, would not be reducible to judicious--but doxastically noncommittal--action policies. Finally, such misbeliefs would have been adaptive in themselves, constituting more than mere by-products of adaptively biased misbelief-producing systems. We explore a range of potential candidates for evolved misbelief, and conclude that, of those surveyed, only positive illusions meet our criteria. Keywords: adaptive; belief; delusions; design; evolution; misbelief; positive illusions; religion; self-deception doi:10.1017/S0140525X09990975

Abstract: The 2:1 adduct of benzyne with 2-methylanisole is shown to have the bisbenzotricyclic structure 6,6a,11,11a-tetrahydro-5-methoxy-6-methyl-5,6,11-metheno-5H-benzo[a]fluorene by a single-crystal X-ray diffraction study ([C.sub.20][H.sub.18]O: [Pca2.sub.1], a = 15.0497(17), b = 9.87783(11), [...]

Research has been conducted on the regulatory domains of the skeletal and cardiac troponin C. The coupling mechanism of troponin structural opening and ligand binding involved in the regulation of skeletal and cardiac muscle contraction has been investigated.

Multinuclear, multidimensional NMR spectroscopy was used to determine the structure of the regulatory domain of chicken skeletal troponin-C (residues 1-90) when combined with the major inhibitory region (residues 96-148) of chicken skeletal troponin-I. The troponin-I peptide-binding site was observed in the hydrophobic pocket of calcium saturated troponin-C, and was found to bind to the regulatory domain of troponin-C in a similar way to a shorter troponin-I peptide.

Picornaviral 3C proteinases have a structure that is a hybrid between thiol proteinase of the papain family and the mammalian serine proteinases. The picornaviral family consists of a group of thiol proteinases that cause the cleaving of viral polyproteins into their component proteins. The picornaviral 3C enzymes catalyze peptide-bond cleavage and the structures of hepatitis A virus (HAV) and human rhinovirus (HRV) indicate that these enzymes are different from the papain family. Peptide-aldehyde is an inhibitor of HAV 3C.

Several studies are conducted to analyse the catalytic proficiency exhibited by the different ubiquitin conjugation enzymes. The various chemical steps involved in the ubiquitination of a compound by achieving a balanced p[k.sub.a] rates are also explained.

Multidimensional NMR studies on subtilosin A, a bacteriocin from Bacillus subtilis, are carried out to determine the complete primary and three-dimensional solution structure of peptide. Results depicted a cyclized peptide backbone with three cross-links formed between the sulfurs of Cys13, Cys 7, and Cys4 and the alpha-positions of Phe22, Thr28 and Phe31 that are showing L form of stereochemistry.