Thermal and cryogenic design study for space infrared telescope facility (SIRTF)

A study was conducted to determine the ability of an all superfluid helium design to meet the performance requirements of background limited to 200 micrometer, and a two year lifetime for a one meter class free flying infrared observatory. Both a 98 deg and 28.5 deg inclination orbits were examined, and aperture shade designs were developed for both orbits. A unique forebaffle cooling design significantly reduces the sensitivity to aperture heat loads. With certain restrictions on observing modes, the study determined that an all superfluid helium Dewar will meet the temperature and lifetime requirements. A dual cryogen SFHe/SH2 system was also investigated for the 28.5 deg orbit and found to provide a more constant forebaffle temperature but with only a slight improvement in lifetime

Circular Dichroism Spectroscopy in the Undergraduate Curriculum

Circular dichroism spectropolarimetry (CD) is a method of optical spectroscopy that seems in most practical ways like UV−visible spectroscopy. The main difference between the two methods is that CD, instead of measuring the absorbance of light as a function of wavelength, measures the difference in absorbance of left versus right circularly polarized light as a function of wavelength. A CD spectrum is an observation of the structure of a chiral compound; it often serves as a “fingerprint” of the structure of biological molecules such as proteins and nucleic acids. For this reason, CD has been broadly applied in biochemistry and in many other areas ranging from organometallic to nanoscale chemistry. Despite its exceptional ease of use and connection to central topics in chemistry, however, CD remains rare in the undergraduate curriculum. This article briefly introduces the theory and practice of CD spectroscopy and a discussion of its advantages in the undergraduate curriculum and the required instrumentation

Cucurbit[8]uril Rotaxanes

The synthesis of [2]rotaxanes, each comprising a viologen core threaded through a cucurbit[8]uril (Q8, Figure 1) macrocycle and stoppered by tetraphenylmethane groups, and their binding to second guests as inclusion complexes in organic and aqueous media are described. Stoppering was observed to have little effect on binding. Chemical modification of the threaded guest was used to control solubility and binding characteristics, thus demonstrating a novel approach to making artificial receptors with readily modifiable properties

Lymphoma and hypercalcemia in a pediatric orthotopic liver transplant patient

We present a case report of a pediatric orthotopic liver transplant recipient who developed lymphoma with hypercalcemia on cyclosporine and prednisone immunosuppression. This is the first reported posttransplant lymphoproliferative disorder complicated by hypercalcemia, with a finding of an elevated 1,25 dihydroxyl vitamin D state, suggesting that it has a role in the pathophysiology of this B cell lymphoma hypercalcemia. The clinical course and management of this disorder with a 31-month follow-up are described. © 1989 by Williams & Wilkins

Sequence-Specific Inhibition of a Nonspecific Protease

A nonspecific exopeptidase, aminopeptidase N (APN), is inhibited sequence-specifically by a synthetic host, cucurbit[7]uril (Q7), which binds with high affinity and specificity to N-terminal phenylalanine (Phe) and 4-(aminomethyl)phenylalanine (AMPhe) and prevents their removal from the peptide. Liquid chromatography experiments demonstrated that in the presence of excess Q7, APN quantitatively converts the pentapeptides Thr-Gly-Ala-X-Met into the dipeptides X-Met (X = Phe, AMPhe). The resulting Q7-bound products are completely stable to proteolytic digestion for at least 24 h. Structure–activity studies revealed a direct correlation between the extent of protection of an N-terminal amino acid and its affinity for Q7. Therefore, Q7 provides predictable sequence-specificity to an otherwise nonspecific protease and enables the production of a single peptide product. Conversely, APN uncovers a high-affinity epitope that is subsequently bound by Q7, and thus this approach should also facilitate the molecular recognition of peptides