1,133 research outputs found
The good parodist: beyond images of escape in the fiction of Doris lessing
No full textIn her earlier fiction, Doris Leasing presents images of escape from what Cohen and Taylor term "everyday life”. These images of escape, such as the vision of the "noble city, set four-square" in Martha Quest and Martha's plunge into the muddy veld pothole in A Proper Marriage, are framed by realism. In positing an escape from 'realism'(understood as both literary form and "everyday reality") they suggest the inadequacy of realism. However, the success of these images is limited as they attempt to posit an "outside", a project which postmodernism has taught us, is bound to fail. Lessing increasingly replaces these images of escape with parody. Parody more fundamentally interrogates realism and allows Lessing to negotiate an escape whilst recognizing her implication in contemporary society. My model of parody takes its lead from Linda Hutcheon's consideration of "serious parody", as marking "the intersection of creation and re-creation, of invention and critique" (A Theory of Parody, 1985). This, I argue, is the intersection of Lessing's political and aesthetic projects. Lessing's use of parody also provides her with a useful strategy for negotiating subjectivity. I argue that whilst she questions the liberal humanist self, she does not completely reject it. She is "post-humanist" rather than "anti-humanist". Lessing's "space fiction" seems to signal a return to the project of positing an "outside" implied by her images of escape. However, I illustrate how her space fiction is equally subject to the problematic politics of parody. Just as parody "installs" a pre-existing text to "subvert" it, so space fiction "installs" the Earth in order to critique it. The "dual-codedness" of parody is, I conclude, perfect for Lessing's multiple projects
DORIS-MAE-v1
No full textIn scientific research, the ability to effectively retrieve relevant documents based on complex, multifaceted queries is critical. Existing evaluation datasets for this task are limited, primarily due to the high costs and effort required to annotate resources that effectively represent complex queries. To address this, we propose a novel task, Scientific DOcument Retrieval using Multi-level Aspect-based quEries (DORIS-MAE), which is designed to handle the complex nature of user queries in scientific research.
Documentations for the DORIS-MAE dataset is publicly available at https://github.com/Real-Doris-Mae/Doris-Mae-Dataset. This upload contains both DORIS-MAE dataset version 1 and ada-002 vector embeddings for all queries and related abstracts (used in candidate pool creation). DORIS-MAE dataset version 1 is comprised of four main sub-datasets, each serving distinct purposes.
The Query dataset contains 100 human-crafted complex queries spanning across five categories: ML, NLP, CV, AI, and Composite. Each category has 20 associated queries. Queries are broken down into aspects (ranging from 3 to 9 per query) and sub-aspects (from 0 to 6 per aspect, with 0 signifying no further breakdown required). For each query, a corresponding candidate pool of relevant paper abstracts, ranging from 99 to 138, is provided.
The Corpus dataset is composed of 363,133 abstracts from computer science papers, published between 2011-2021, and sourced from arXiv. Each entry includes title, original abstract, URL, primary and secondary categories, as well as citation information retrieved from Semantic Scholar. A masked version of each abstract is also provided, facilitating the automated creation of queries.
The Annotation dataset includes generated annotations for all 165,144 question pairs, each comprising an aspect/sub-aspect and a corresponding paper abstract from the query's candidate pool. It includes the original text generated by ChatGPT (version chatgpt-3.5-turbo-0301) explaining its decision-making process, along with a three-level relevance score (e.g., 0,1,2) representing ChatGPT's final decision.
Finally, the Test Set dataset contains human annotations for a random selection of 250 question pairs used in hypothesis testing. It includes each of the three human annotators' final decisions, recorded as a three-level relevance score (e.g., 0,1,2).
The file "ada_embedding_for_DORIS-MAE_v1.pickle" contains text embeddings for the DORIS-MAE dataset, generated by OpenAI's ada-002 model. The structure of the file is as follows:
├── ada_embedding_for_DORIS-MAE_v1.pickle
├── "Query"
│ ├── query_id_1 (Embedding of query_1)
│ ├── query_id_2 (Embedding of query_2)
│ └── query_id_3 (Embedding of query_3)
│ .
│ .
│ .
└── "Corpus"
├── corpus_id_1 (Embedding of abstract_1)
├── corpus_id_2 (Embedding of abstract_2)
└── corpus_id_3 (Embedding of abstract_3)
.
.
.The DORIS-MAE dataset is contained in a paper submitted to NeurIPS 2023 Dataset Track for review. Please refer to benchmarking details in the GitHub link: https://github.com/Real-Doris-Mae/Doris-Mae-Dataset. Author information will be made available shortly
represents a novel type of binding domain with affinity for soluble xylan and mixed‐linkage β‐1,3/β‐1,4‐glucan
No full textThermotoga maritima XynA is an extremely thermostable modular enzyme with five domains (A1-A2-B-C1-C2), Its catalytic domain (-B-) is flanked by duplicated non-catalytic domains, The C-terminal repeated domains represent cellulose-binding domains (CBDs), Xylanase domains related to the N-terminal domains of XynA (A1-A2) are called thermostabilizing domains because their deletion normally leads to increased thermosensitivity of the enzymes. It was found that a glutathione-S-transferase (GST) hybrid protein (GST-A1A2) containing both A-domains of XynA can interact with various soluble xylan preparations and with mixed-linkage beta-1,3/beta-1,4-glucans, GST-A1A2 showed no affinity for insoluble microcrystalline cellulose, whereas, vice versa, GST-CP, which contains the C-terminal CBD of XynA, did not interact with soluble xylan, Another hybrid protein, GST-AS, displayed the same binding properties as GST-A1A2, indicating that A2 alone can also promote xylan binding. The dissociation constants for the binding of xylose, xylobiose, xylotriose, xylotetraose and xylopentaose by GST-AP, as determined at 20 degrees C by fluorescence quench experiments, were 8.1 x 10(-3) M, 2.3 x 10(-4) M, 2.3 x 10(-5) M, 2.5 x 10(-6) M and 1.1 x 10(-6) M respectively. The A-domains of XynA, which are designated as xylan binding domains (XBD), are, from the structural as well as the functional point of view, prototypes of a novel class of binding domains. More than 50 related protein segments with hitherto unknown function were detected in about 30 other multidomain beta-glycanases, among them putative plant (Arabidopsis thaliana) xylanases, It is argued that polysaccharide binding and not thermostabilization is the main function of A-like domains
Letter From Ruby Doris Smith to her Mother, circa 1964
No full textCorrespondence from Ruby Doris Smith to her mother about being in Conakry, Guinea in West Africa. 4 pages
Mary Ann Smith Wilson, Ruby Doris Smith Robinson Collection on Student Activism
No full textThe Mary Ann Smith Wilson - Ruby Doris Smith Robinson Collection on Student Activism spans the dates 1948-2008 with the bulk of the material dated 1960-1967. The collection documents both Ruby Doris Smith Robinson's and Mary Ann Smith Wilson's participation in the civil rights movement and the organizations with which they were affiliated. Although the collection documents both sisters' activities, the bulk of the collection reflects Ruby Doris Smith Robinson’s activism activities in the civil rights movement. Also included in the collection are photographs, correspondences, news articles, programs, reports, and flyers.
At the AUC Robert W. Woodruff Library, we are always striving to improve our digital collections. We welcome additional information about people, places, or events depicted in any of the works in this collection. To submit information, please contact us at [email protected]
Maltose-binding protein from the hyperthermophilic bacterium Thermotoga maritima: Stability and binding properties
No full textRecombinant maltose-binding protein from Thermotoga maritima (TmMBP) was expressed in Escherichia coli and purified to homogeneity, applying heat incubation of the crude extract at 75 degrees C. As taken from the spectral, physicochemical and binding properties, the recombinant protein is indistinguishable from the natural protein isolated from the periplasm of Thermotoga maritima. At neutral pH, TmMBP exhibits extremely high intrinsic stability with a thermal transition >105 degrees C. Guanidinium chloride-induced equilibrium unfolding transitions at varying temperatures result in a stability maximum at approximate to 40 degrees C. At room temperature, the thermodynamic analysis of the highly cooperative unfolding equilibrium transition yields Delta G(N) --> (U) 100(+/-5) kJ mol(-1) for the free energy of stabilization. Compared to mesophilic MBP from E. coli as a reference, this value is increased by about 60 kJ mol(-1). At temperatures around the optimal growth temperature of T. maritima (t(opt) approximate to 80 degrees C), the yield of refolding does not exceed 80%; the residual 20% are misfolded, as indicated by ii decrease in stability as well as loss of the maltose-binding capacity. TmMBP is able to bind maltose, maltotriose and trehalose with dissociation constants in the nanomolar to micromolar range, combining the substrate specificities of the homologs from the mesophilic bacterium E.coli and the hyperthermophilic archaeon Thermococcus litoralis. Fluorescence quench experiments allowed the dissociation constants of Ligand binding to be quantified. Binding of maltose was found to be endothermic and entropy-driven, with Delta H-b = + 47 kJ mol(-1) and Delta S-b = + 257 J mol(-1) K-1. Extrapolation of the linear vant 'Hoff plot to t(opt) resulted in K-d approximate to 0.3 mu M. This result is in agreement with data reported for: the MBPs from E, coli and T, litoralis at their respective optimum growth temperatures, corroborating the general observation that proteins under their specific physiological conditions are in corresponding states. (C) 2000 Academic Press
Letter From Ruby Doris Smith to Her Sister Mary Ann Smith, February 25, 1961
No full textCorrespondence from Ruby Doris Smith to her sister Mary Ann Smith from York County Jail. 5 pages
Author Doris Lessing
No full textDoris Lessing was the keynote speaker on Opening day of the National Word Festival 198
Doris Burton
No full textDoris Karren Burton was born to Victor and Stella Karren on March 16, 1932. She married Troy Burton in 1951. Doris was a talented woman. She was a musician and an author. She was the Uintah County Librarian and later the director of the Regional History Center which she began. She recieved many awards for her talents and work. Doris died June 17, 2015
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