A conventional point of view on active magnetic bearings

Active magnetic bearings used in rotating machinery should be designed as locally controlled, independent devices similar to other types of bearings. The functions of control electronics and power amplifiers can be simply and explicitly related to general bearing properties such as load capacity, stiffness, and damping. The dynamics of a rotor and its supporting active magnetic bearings are analyzed in a modified conventional method with an extended state vector containing the bearing state variables

Metropolitan Briefing Book, 2007

The Institute of Portland Metropolitan Studies (IMS) was created to connect the resources of higher education to the needs of the six-county, bit-state Portland-Vancouver metropolitan area (Clackamas, Clark, Columbia, Multnomah, Washington, and Yamhill Counties). In this spirit, we offer our 2007 Metropolitan Briefing Book. Our theme is regional variety. Variety has been touted as the very spice of life (William Cowper) and as the mother of enjoyment (Vivan Grey). Our region enjoys a good deal of variety--in its landscapes, in its economy, and in its people, their cultures, and their attitudes. These differences are important to local vitality and beauty. But while we generally view this variety as positive, we also worry about equity. Although we promote regional thought and action, we must understand that each community experiences the problems facing us in a slightly different way and often with significantly different resources

Explorations, Vol. 5, No. 1

Articles include: Cover: What Have We Done with Tomorrow? by Leslie C. Hyde, UMCES Extension Agent for Knox-Lincoln Counties. Editorial Reflections, Carole J. Bombard UMCES: an overview Conversation with the Director: Assistant Vice-President Judith Bailey Reaching Out for Teen Awareness, by Theresa M. Ferrari Profile of a Harbormaster, by Carole J. Bombard Minding Maine’s Business, by Mary S. Bowie Family Resource Management: Learning to ease the burden, by Olive Dubord and Doris Cushman Breaking Free and Taking Control: Helen Sawyer’s Story, by Doris Manley Partnership in Conservation: The Josephine Newman Sanctuary, by Nancy Coverstone The Mount Desert Island Health Promotion Project, by Ron Beard Dynamics of Weed Control in Agriculture, by Leigh Morrow From Generation to Generation: An Extension Homemaker Family, by Nadine B. Reimer ICLAD: The Institute for Community Leadership and Development, by Jim Killacky and Deb Burwell Exploding the Cinderella Syndrome: Strengthening Stepfamilies, by Wendy Pollock Integrated Pest Management: Bringing it all together, by Glen Koehler and Jim Dill Addressing the Issues, by Patricia M. Pierson Anti-Bruise: What’s It All About? Maine Potato Harvest Anti-Bruise Program, by Neal D. Hallee H.O.P.E. Addresses Teenage Pregnancy, by Jane M. Kelly Saving Money and the Environment, by Vaughn H. Holyoke Reservoir Tillage in Nonirrigated Potato Production, by Leigh Morrow Managing Pesticide Drift, by James D. Dwyer, Leigh S. Morrow and James F. Dill The St. George River Project — what have we done with tomorrow? Putting Research to Work, by Stephen Belyea The Best Maine Blue: Fresh Pack Blueberries, by Tom DeGomez Maine’s Green Sea Urchin, by Benjamin A. Baxter Interfaces and Cooperation: Wildlife and Fisheries Sampler, by Catherine A. Elliott Extension Responds to the Salmonella Scare, by Nellie Hedstrom and Mahmoud El-Begearm

A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis

Great strides into understanding protein folding have been made since he seminal work of Anfinsen over 40 years ago, but progress in the study of membrane protein folding has lagged behind that of their water soluble counterparts. Researchers in these fields continue to turn to more advanced techniques such as NMR, mass spectrometry, molecular dynamics (MD) and single molecule methods to interrogate how proteins fold. Our understanding of β-barrel outer membrane protein (OMP) folding has benefited from these advances in the last decade. This class of proteins must traverse the periplasm and then insert into an asymmetric lipid membrane in the absence of a chemical energy source. In this review we discuss old, new and emerging techniques used to examine the process of OMP folding and biogenesis in vitro and describe some of the insights and new questions these techniques have revealed

The effect of artificial selection on phenotypic plasticity in maize

Remarkable productivity has been achieved in crop species through artificial selection and adaptation to modern agronomic practices. Whether intensive selection has changed the ability of improved cultivars to maintain high productivity across variable environments is unknown. Understanding the genetic control of phenotypic plasticity and genotype by environment (G × E) interaction will enhance crop performance predictions across diverse environments. Here we use data generated from the Genomes to Fields (G2F) Maize G × E project to assess the effect of selection on G × E variation and characterize polymorphisms associated with plasticity. Genomic regions putatively selected during modern temperate maize breeding explain less variability for yield G × E than unselected regions, indicating that improvement by breeding may have reduced G × E of modern temperate cultivars. Trends in genomic position of variants associated with stability reveal fewer genic associations and enrichment of variants 0–5000 base pairs upstream of genes, hypothetically due to control of plasticity by short-range regulatory elements

A molecular marker for, and the organization of, a cluster of loose smut resistance genes in oat

Loose smut (Ustilago avenae) resistance breeding is hampered by the many distinct smut races, and the different, poorly characterized resistance genes. Three pathotypes (A13, A60, A617) represent the most common races present in the prairie regions of western Canada (Kibite et al. 2000). Markers linked to a group of smut resistance genes located on linkage group 14 (Kanota/ Ogle) have been developed (Eckstein et al. 2002). One co-dominant SCAR marker was used to study the relationship between the marker and the three resistance genes. Molecular markers and plant populations used were described in Eckstein et al. (2002). Another population (OT369/89Ab4088) segregating for the three genes was also evaluated. All lines were inoculated with separate isolates of A13, A60, and A617 using a vacuum protocol, and grown over several locations and years in western Canada. SCAR marker Ua300co (co-dominant) was linked (~ 5 cM) to a resistance gene specific for pathotype A13. Two other pathotype specific genes clustered on the same side of the marker at genetic distances of 8 cM (A617) and 18 cM (A60). The genes are linked in coupling and are likely often inherited as a group. Attempts to find a flanking marker for the cluster are in progress. Eckstein et al. 2002. In: American Oat Workers Conference, Wilmington, NC, USA, May 5-7, 2002. pp33; Kibite et al. 2000. In: Cross, R.J. (ed). Proceedings of the 6th International Oat Conference, Lincoln, NZ. November 13-16 2000. pp298-301.vokMyynti MTT tietopalvelu

Ultrafast hydration dynamics in protein unfolding: Human serum albumin

We report studies of unfolding and ultrafast hydration dynamics of the protein human serum albumin. Unique in this study is our ability to examine different domains of the same protein and the intermediate on the way to the unfolded state. With femtosecond resolution and site-selective labeling, we isolate the dynamics of domains I and II of the native protein, domain I of the intermediate at 2 M guanidine hydrochloride, and the unfolded state at 6 M of the denaturant. For studies of unfolding, we used the fluorophores, acrylodan (covalently bound to Cys-34 in domain I) and the intrinsic tryptophan (domain II), whereas for hydration dynamics, we probed acrylodan and prodan; the latter is bound to domain II. From the time-dependent spectra and the correlation functions, we obtained the time scale of dynamically ordered water: 57 ps for the more stable domain I and 32 ps for the less stable domain II, in contrast to ≈0.8 ps for labile, bulk-type water. This trend suggests an increased hydrophilic residues–water interaction of domain I, contrary to some packing models. In the intermediate state, which is characterized by essentially intact domain I and unfolded domain II, the dynamics of ordered water around domain I is nearly the same (61 ps) as that of native state (57 ps), whereas that in the unfolded protein is much shorter (13 ps). We discuss the role of this fluidity in the correlation between stability and function of the protein