North American Jewish Students Appeal records, undated, 1962, 1964-1996 (bulk 1971-1995)

The records of the North American Jewish Students Appeal (NAJSA or APPEAL) contains documents on two levels of concern: those documents dealing with the NAJSA as a student-run organization promoting Jewish identity among college-aged youth; and those documents dealing with the APPEAL as a fundraising organization for several well-known student constituent organizations. The Constituents were: the Jewish Student Press Service, Lights in Action, the North American Jewish Students Network, the Progressive Zionist Caucus, Response: A Contemporary Jewish Review, Yavneh Religious Students Organization, and Yugntruf Youth for Yiddish. Documents include correspondence, financial records, minutes, press releases, information on grants awarded to student organizations for programming and publishing, student journals, and newspapers, photographs, and ephemera.

Congregation Shearith Israel (New York, N.Y.) records, undated, 1755-1996.

Contains published and manuscript material relating to the activities and administration of the congregation and its subsidiary organizations including reports and weekly bulletins, early financial records and lists of those honored at religious services, copies of resolutions and forms of service and prayers for various occasions in manuscript form. Contains also material relating to the cemetery photographs, the Hebra Hased Va-Amet (the congregational burial society) and to later clergy in the congregation, Henry Pereira Mendes, David de Sola Pool and Louis Coleman Gerstein including published copies of their sermons.

Temple Israel Boston, Massachusetts collection, 1924-1996

Temple Israel was founded as Congregation Adath Israel in 1854 when a group of German Jews broke from Congregation Ohabei Shalom. The congregation was also known as the Pleasant Street Synagogue. In 1859, the congregation purchased cemetery land in Wakefield, Massachusetts. The synagogue was, and remains, a Reform congregation, and has been home to well known Rabbis, including Joshua Loth Liebman and Roland B. Gittelsohn. This collection contains flyers, newsletters, pamphlets, sermons and a yearbook.

Upper Valley Jewish Community Hanover, New Hampshire collection, undated, 1984-1996

The Upper Valley Jewish Community (UVJC) is an egalitarian congregation on the campus of Dartmouth College. The congregation hosts a Hebrew School and publishes the newsletter, "The Jewish Connection." This collection consists of several issues of the publication, "The Jewish Connection," as well as other miscellaneous invitations and programs for a variety of events.

Hebrew College collection, 1928-1996

Louis Hurwich, then superintendent of the Bureau of Jewish Education of Boston, founded Hebrew Teacher’s College in 1921. Hurwich was concerned about Jewish teachers leaving the field of Jewish education for other professions and sought an educational system that promoted Hebrew literacy at all levels. Hebrew Teacher’s College was also responsible for maintaining Hebrew High School (Prozdor), located at 14 Crawford Street in Roxbury, Massachusetts. Those students who graduated from the high school could matriculate to Hebrew Teacher’s College without having to take an exam. In 1943, the high school offered Talmud classes in addition to its regular curriculum, with studies in the Bible, Hebrew, Jewish History, and codes and customs. In 2002, the College moved to its current location in Newton, Massachusetts. One year later, it opened its Rabbinical School. This collection contains brochures, catalogs, commencement addresses, event fliers, invitations, pamphlets and publications.

Temple Mishkan Tefila Boston, Massachusetts collection, 1922-1996

Congregation Mishkan Tefila was founded in 1858 as Mishkan Israel, and is considered to be the oldest conservative synagogue in New England. Its founding members were East Prussian Jews who separated from Ohabei Shalom, which was predominately Polish at the time. In 1894, Mishkan Israel and another conservative synagogue, Shaarei Tefila, merged to form Congregation Mishkan Tefila. The synagogue moved its religious school to Walnut Street in Newton in 1955, and began planning for a new building in Chestnut Hill on Hammond Pond Parkway. The groundbreaking ceremony was on November 13, 1955. In 1958, services were held for the first time in the new synagogue building. This collection contains plays, annual reports, programs for events and dinners, and newsletters.

Herbert Leiser Collection 1932-1946

Zeitschrift K.C. Blaetter (1932-1933); Festschrift of K.C., New York, 1946; Literaturwegweiser fuer den K.C., Berlin 1926; Hochschulhefte, 1921; misc. printings and publications of the K.C. including fraternity postcards with logos; clipping about the voyage of ship to St. Louis (1939).

Marianne Berel Collection 1938-1996

Clippings, correspondence, published and unpublished articles on learning disabilities and music therapy; contains testimony on her experience in the internment camp of Gurs, France.

Erna Proskauer Collection 1988-1996

The collection contains published materials in honor of Erna Proskauer and her career in law. Also included are speeches and correspondence pertaining to her receiving the German medal of honor, Bundesverdienstkreuz, on April 5, 1995.

Water stress induced alterations in ornithine aminotransferase of ragi (Eleusine coracana): Protection by proline against heat inactivation and denaturation by urea and guanidinium chloride

Water stress resulted in a specific response leading to a large and significant increase (80-fold) in free proline content of ragi (Eleusine coracana) leaves and seedlings. L-Proline protected ornithine aminotransferase, an enzyme in the pathway for proline biosynthesis, isolated from normal and stressed ragi leaves against heat inactivation and denaturation by urea and guanidinium chloride. The protection of the stressed enzyme by L-proline was much more complete than that of the enzyme isolated from normal leaves. While L-ornithine, one of the substrates, protected the stressed enzyme against inactivation, it enhanced the rate of inactivation of the normal enzyme. α-Ketoglutarate protected both the normal and stressed enzyme against inactivation and denaturation. These results support the suggestion that ornithine aminotransferase has undergone a structural alteration during water stress. In view of the causal relationship between elevated temperature and water stress of plants under natural conditions, the protection afforded by proline against inactivation and denaturation of the enzyme from stressed leaves assumes significance. These results provide an explanation for a possible functional importance of proline accumulation during water stress.

Annual nitrogen dynamics and urea fertilizer recoveries from a dairy pasture using 15N; effect of nitrification inhibitor DMPP and reduced application rates

Direct nitrogen (N) losses from pastures contribute to the poor nitrogen use efficiency of the dairy industry, though the exact fate of applied N and the processes involved are largely unknown. Nitrification inhibitors such as DMPP can potentially increase fertilizer N use efficiency (NUE), though few studies globally have examined the effectiveness of DMPP coated urea in pastures. This study quantified the NUE of DMPP combined with reduced application rates, and the effect on N dynamics and plant–soil interactions over an annual ryegrass/kikuyu rotation in Queensland, Australia. Labeled 15N urea and DMPP was applied over 7 winter applications at standard farmer (45 kg N ha−1) and half (23 kg N ha−1) rates. Fertilizer recoveries and NUE were calculated over 13 harvests, and the contribution of fertilizer and soil N estimated. Up to 85% of the annual N harvested was from soil organic matter. DMPP at the lower rate increased annual yields by 31% compared to the equivalent urea treatment with no difference to the high N rates. Almost 40% of the N added at the conventional fertilizer application rate as urea was lost to the environment; 80 kg N ha−1 higher than the low DMPP. Combining the nitrification inhibitor DMPP with reduced fertilizer application rates shows substantial potential to reduce N losses to the environment while sustaining productivity in subtropical dairy pastures.

Covalent tethering of the dimer interface annuls aggregation in thymidylate synthase

Thymidylate synthase (TS), a dimeric enzyme, forms large soluble aggregates at concentrations of urea (3.3-5 M), well below that required for complete denaturation, as established by fluorescence and size-exclusion chromatography. In contrast to the wild-type enzyme, an engineered mutant of TS (T155C/E188C/C244T), TSMox, in which two subunits are crosslinked by disulfide bridges between residues 155-188' and 188-155', does not show this behavior. Aggregation behavior is restored upon disulfide bond reduction in the mutant protein, indicating the involvement of interface segments in forming soluble associated species. Intermolecular disulfide crosslinking has been used as a probe to investigate the formation of larger non-native aggregates. The studies argue for the formation of large multimeric species via a sticky patch of polypeptide from the dimer interface region that becomes exposed on partial unfolding. Covalent reinforcement of relatively fragile protein-protein interfaces may be a useful strategy in minimizing aggregation of non-native structures in multimeric proteins.

Unfolding of Plasmodium falciparum Triosephosphate Isomerase in Urea and Guanidinium Chloride: Evidence for a Novel Disulfide Exchange Reaction in a Covalently Cross-Linked Mutant†

The conformational stability of Plasmodium falciparum triosephosphate isomerase (TIMWT) enzyme has been investigated in urea and guanidinium chloride (GdmCl) solutions using circular dichroism, fluorescence, and size-exclusion chromatography. The dimeric enzyme is remarkably stable in urea solutions. It retains considerable secondary, tertiary, and quaternary structure even in 8 M urea. In contrast, the unfolding transition is complete by 2.4 M GdmCl. Although the secondary as well as the tertiary interactions melt before the perturbation of the quaternary structure, these studies imply that the dissociation of the dimer into monomers ultimately leads to the collapse of the structure, suggesting that the interfacial interactions play a major role in determining multimeric protein stability. The C-m(urea)/C-m(GdmCl) ratio (where C-m is the concentration of the denaturant required at the transition midpoint) is unusually high for triosephosphate isomerase as compared to other monomeric and dimeric proteins. A disulfide crosslinked mutant protein (Y74C) engineered to form two disulfide cross-links across the interface (13-74') and (13'-74) is dramatically destablized in urea. The unfolding transition is complete by 6 M urea and involves a novel mechanism of dimer dissociation through intramolecular thiol-disulfide exchange.

N-H center dot center dot center dot O and C-H center dot center dotcenter dot O interaction mimicry in the 1:1 molecular complexes of 5,5-diethylbarbituric acid with urea and acetamide

The analogy between N-H center dot center dot center dot O and C-H center dot center dot center dot O intermolecular interactions is studied with variable temperature (180-100 K) single crystal X-ray diffraction analysis.5,5-Diethylbarbituric acid (barbital) forms isostructural molecular complexes (co-crystals) with urea (1) and acetamide (2) that respectively contain these analogous interactions.The behaviour of these two interactions as a function of temperature is very similar. This indicates that the C-H center dot center dot center dot O bond in barbital acetamide plays a similar chemical and structural role as does the N-H center dot center dot center dot O bond in barbital urea. The close relationship between these interactions and their comparable nature is further adduced from the formation of a ternary solid solution (3) of barbital, urea and acetamide. The fact that the C-H center dot center dot center dot O interaction in barbital acetamide is weaker than the N-H center dot center dot center dot O interaction in barbital urea is shown by the fact that acetamide is under expressed and urea is over expressed with respect to the quantities of these substances present in solution prior to crystallization of these ternary crystals.