Campus Environment 2008: A National Report Card on Sustainability in Higher Education

Presents survey findings on national and regional trends among colleges in environmental leadership in management, academic courses in sustainability, and conservation efforts in operations. Profiles exemplary programs and notes areas for improvement

Cost-effective use of liquid nitrogen in cryogenic wind tunnels, phase 2

Cryogenic seal tests were performed and Rulon A was selected for the subject nutating positive displacement expander. A four-chamber expander was designed and fabricated. A nitrogen reliquefier flow system was also designed and constructed for testing the cold expander. Initial tests were unsatisfactory because of high internal friction attributed to nutating Rulon inlet and outlet valve plates. Replacement of the nutating valves with cam-actuated poppet valves improved performance. However, no net nitrogen reliquefaction was achieved due to high internal friction. Computer software was developed for accurate calculation of nitrogen reliquefaction from a system such as that proposed. These calculations indicated that practical reliquefaction rates of 15 to 19 percent could be obtained. Due to mechanical problems, the nutating expander did not demonstrate its feasibility nor that of the system. It was concluded that redesign and testing of a smaller nutating expander was required to prove concept feasibility

An investigation of CdS thin films and germanium-CdS-copper switching devices

Summary: p. vii

Structural Basis for α-Conotoxin Potency and Selectivity

Parkinson\u27s disease is a debilitating movement disorder characterized by altered levels of α6β2* nicotinic acetylcholine receptors (nAChRs) localized on presynaptic striatal catecholaminergic neurons. α-Conotoxin MII (α-CTx MII) is a highly useful ligand to probe α6ß2 nAChRs structure and function, but it does not discriminate among closely related α6* nAChR subtypes. Modification of the α-CTx MII primary sequence led to the identification of α-CTx MII[E11A], an analog with 500-5300 fold discrimination between α6* subtypes found in both human and non-human primates. α-CTx MII[E11A] binds most strongly (femtomolar dissociation constant) to the high affinity α6* nAChR, a subtype that is selectively lost in Parkinson\u27s disease. Here we present the three-dimensional solution structure for α-CTx MII[E11A] as determined by two-dimensional 1H NMR spectroscopy to 0.13 +/- 0.09 Ǻ backbone and 0.45 +/- 0.08 Ǻ heavy atom root mean square deviation from mean structure. Structural comparisons suggest that the increased hydrophobic area of α-CTx MII[E11A] relative to other members of the α-CTx family may be responsible for its exceptionally high affinity for α6α4β2* nAChR as well as discrimination between α6ß2 and α3β2 containing nAChRs. This finding may enable the rational design of novel peptide analogs that demonstrate enhanced specificity for α6* nAChR subunit interfaces and provide a means to better understand nAChR structural determinants that modulate brain dopamine levels and the pathophysiology of Parkinson\u27s disease