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Many sequencing and scheduling problems can be formulated as 0-1 integer programs and, in theory, solved using a branch-and-bound approach. In practice, real-world instances of these problems are usually solved using heuristics. In this paper we demonstrate the benefits of incorporating an intuitive, user-controlled variable-tolerance into a depth-first branch-and-bound algorithm. The tolerance comprises two components: a variable depth tolerance and a variable breadth tolerance. A sample scheduling problem is thoroughly analysed to illustrate empirically parameter impact on solution quality and execution time. Then, results based on several real-world problems are discussed.

Some promising biomass clones traded in Great Britain as Salix x smithiana Willd. (S. viminalis x S. cinerea) are in fact S. x sericans Tausch ex Kern. (S. viminalis x S. caprea) but the major problem discussed is that two distinct willows are masquerading under the same name, S. dasyclados. To avoid confusion it is suggested that S. x dasyclados Wimmer is retained for the hybrid (2n = 57), a female clone and formerly a notable Dutch and English basket willow, whereas for S. dasyclados Skvortsov non Wimmer, a species ranging from the Baltic to Siberia with 2n = 76, the name S. burjatica Nasarov, as suggested by Chmelar, is preferred. The willows distributed and designated Salix aquatica Gigantea by the Danish willows specialist Jensen, which formed the basis of many early biomass trials, are regarded at present as selections of, or very similar to, S. burjatica Nasarov (S. dasyclados sensu Skvortsov non Wimmer). In addition to a higher level of ploidy, they are visually distinguishable from S. x dasyclados Wimm. by their wider and longer leaves, persistent stipules and the existence of male forms.

Many transcription factors and some other proteins contain glutamine repeats; their abnormal expansion has been linked to several dominantly inherited neuro-degenerative diseases. Having found that poly(L-glutamine) alone forms beta-strands held together by hydrogen bonds between their amide groups, we surmised that glutamine repeats may form polar zippers, an unusual motif for protein-protein interactions. To test this hypothesis, we have engineered a Gly-Gln10-Gly peptide into the inhibitory loop of truncated chymotrypsin inhibitor 2 (CI2), a small protein from barley seeds, by both insertion and replacement. Gel filtration resolved both mutant inhibitors into at least three fractions, which analytical ultracentrifugation identified as monomers, dimers, and trimers of the recombinant protein; the truncated wild-type CI2 formed only monomers. CD difference spectra of the dimers and trimers versus wild type indicated that their glutamine repeats formed beta-pleated sheets, while those of the monomers versus wild type were more suggestive of type I beta-turns. The CD spectra of all three fractions remained unchanged even after incubation at 70 degrees C; neither the dimers nor the trimers dissociated at this temperature. We argue that the stability of all three fractions is due to the multiplicity of hydrogen bonds between extended strands of glutamine repeats in the oligomers or within a beta-hairpin formed by the single glutamine repeat of each monomer. Pathological effects may arise when expanded glutamine repeats cause proteins to acquire excessively high affinities for each other or for other proteins with glutamine repeats.

Coprinus atramentarius was grown on two commercial composts at a constant 20°C or with a cold shock (25°C?20°C) after 10 days. Cold shock was required for it to form fruiting bodies.