De Rham Cohomology and Hodge decomposition for Quantum Groups

Let G=G(t,z) be one of the N^2-dimensional bicovariant first order differential calculi for the quantum groups GL_q(N), SL_q(N), O_q(N), or Sp_q(N), where q is a transcendental complex number and z is a regular parameter. It is shown that the de Rham cohomology of Woronowicz' external algebra G^ coincides with the de Rham cohomologies of its left-coinvariant, its right-coinvariant and its (twosided) coinvariant subcomplexes. In the cases GL_q(N) and SL_q(N) the cohomology ring is isomorphic to the coinvariant external algebra G^_{inv} and to the vector space of harmonic forms. We prove a Hodge decomposition theorem in these cases. The main technical tool is the spectral decomposition of the quantum Laplace-Beltrami operator. Keywords: quantum groups, bicovariant differential calculi, de Rham cohomology, Laplace-Beltrami operator, Hodge theoryComment: LaTeX2e, 40 page

Flexible Automation as a Special Application of Information Technology and Division of Labour

This paper was presented at a joint seminar on flexible automation held in Berlin (East) from June 8-11, 1982. The seminar was a collaborative project between IIASA and the Academy of Sciences of the German Democratic Republic. This paper deals with specific changes brought about by the application of microelectronic components in manufacturing automation

Summer Garden Chat

https://digitalcommons.library.umaine.edu/mmb-ps/1905/thumbnail.jp

OPTIMIZATION OF DISCUS FLIGHT

We use a 3-D model for men’s and women’s discus flight including initial discus flight path angle β0, angle of attack α0, pitch attitude δ0 as well as release speed v0 and initial spin rate p0. We study in detail optimal release conditions depending on a constant wind velocity of v0 =5 m/s blowing from different directions γ=0°, 10° up to 350°. Here γ =0°, 180°, 90°, and 270° correspond to tail wind, head wind, wind from the left, and wind from the right, respectively. The optimal wind for men is head wind from the right (γ= 220°). In this case optimal men’s strategy at v0=25 m/s is β0 = 33°, α0= 23°, δ0= 30° with a range r=74.80 m. Optimal wind for women is wind exactly from the right (γ= 270°). The optimal women’s strategy at v0=24 m/s is β0 = 41°, α0= 32°, δ0 = 30° with a range r=61.26 m. In all cases we assume an initial spin rate of p0=50 rad/s. At the moment of release, the angle of attack α0 of the discus symmetry plane should always be less than the flight path angle β0. Also, we can show that a faster-spinning discus imparts greater gyroscopic stability and therefore achieves a better throw. We used evolutionary algorithms to perform the optimization

The association among diet, dietary fiber, and bowel preparation at colonoscopy

BACKGROUND AND AIMS: Pre-colonoscopy dietary restrictions vary widely and lack evidence-based guidance. We investigated whether fiber and various other foods/macronutrients consumed during the 3 days before colonoscopy are associated with bowel preparation quality. METHODS: This was a prospective observational study among patients scheduled for outpatient colonoscopy. Patients received instructions including split-dose polyethylene glycol, avoidance of vegetables/beans 2 days before colonoscopy, and a clear liquid diet the day before colonoscopy. Two 24-hour dietary recall interviews and 1 patient-recorded food log measured dietary intake on the 3 days before colonoscopy. The Nutrition Data System for Research was used to estimate dietary exposures. Our primary outcome was the quality of bowel preparation measured by the Boston Bowel Preparation Scale (BBPS). RESULTS: We enrolled 201 patients from November 2015 to September 2016 with complete data for 168. The mean age was 59 years (standard deviation, 7 years), and 90% of colonoscopies were conducted for screening/surveillance. Only 17% and 77% of patients complied with diet restrictions 2 and 1 day(s) before colonoscopy, respectively. We found no association between foods consumed 2 and 3 days before colonoscopy and BBPS scores. However, BPPS was positively associated with intake of gelatin, and inversely associated with intake of red meat, poultry, and vegetables on the day before colonoscopy. CONCLUSIONS: Our findings support recent guidelines encouraging unrestricted diets >1 day before colonoscopy if using a split-dose bowel regimen. Furthermore, we found no evidence to restrict dietary fiber 1 day before colonoscopy. We also found evidence to promote consumption of gelatin and avoidance of red meat, poultry, and vegetables 1 day before colonoscopy.Dr Jacobson has acted as a consultant for MOTUS GI and Remedy Partners. All other authors disclosed no financial relationships relevant to this publication. Supported by NIH/NIDDK R21DK105476. (R21DK105476 - NIH/NIDDK)Accepted manuscrip

The creation and early implementation of a high speed fiber optic network for a university health sciences center

pre-printIn late 1989 the University of Missouri Health Sciences Center began the process of creating an extensive fiber optic network throughout its facilities, with the intent to provide networked computer access to anyone in the Center desiring such access, regardless of geographic location or organizational affiliation. A committee representing all disciplines within the Center produced and, in conjunction with independent consultants, approved a comprehensive design for the network. Installation of network backbone components commenced in the second half of 1990 and was completed in early 1991. As the network entered its initial phases of operation, the first realities of this important new resource began to manifest themselves as enhanced functional capacity in the Health Sciences Center. This paper describes the development of the network, with emphasis on its design criteria, installation, early operation, and management. Also included are discussions on its organizational impact and its evolving significance as a medical community resource

Elucidation of Short Linear Motif-Based Interactions of the FERM Domains of Ezrin, Radixin, Moesin, and Merlin

The ERM (ezrin, radixin, and moesin) family of proteins and the related protein merlin participate in scaffolding and signaling events at the cell cortex. The proteins share an N-terminal FERM [band four-point-one (4.1) ERM] domain composed of three subdomains (F1, F2, and F3) with binding sites for short linear peptide motifs. By screening the FERM domains of the ERMs and merlin against a phage library that displays peptides representing the intrinsically disordered regions of the human proteome, we identified a large number of novel ligands. We determined the affinities for the ERM and merlin FERM domains interacting with 18 peptides and validated interactions with full-length proteins through pull-down experiments. The majority of the peptides contained an apparent Yx[FILV] motif; others show alternative motifs. We defined distinct binding sites for two types of similar but distinct binding motifs (YxV and FYDF) using a combination of Rosetta FlexPepDock computational peptide docking protocols and mutational analysis. We provide a detailed molecular understanding of how the two types of peptides with distinct motifs bind to different sites on the moesin FERM phosphotyrosine binding-like subdomain and uncover interdependencies between the different types of ligands. The study expands the motif-based interactomes of the ERMs and merlin and suggests that the FERM domain acts as a switchable interaction hub

Evolution of a fluorinated green fluorescent protein

The fluorescence of bacterial cells expressing a variant (GFPm) of the green fluorescent protein (GFP) was reduced to background levels by global replacement of the leucine residues of GFPm by 5,5,5-trifluoroleucine. Eleven rounds of random mutagenesis and screening via fluorescence-activated cell sorting yielded a GFP mutant containing 20 amino acid substitutions. The mutant protein in fluorinated form showed improved folding efficiency both in vivo and in vitro, and the median fluorescence of cells expressing the fluorinated protein was improved {approx}650-fold in comparison to that of cells expressing fluorinated GFPm. The success of this approach demonstrates the feasibility of engineering functional proteins containing many copies of abiological amino acid constituents