title: A fedora librarian interface

authors: Bainbridge, David

subjects: computer science

abstract: The Fedora content management system embodies a powerful and flexible digital object model. This paper describes a new open-source software front-end that enables end-user librarians to transfer documents and metadata in a variety of formats into a Fedora repository. The main graphical facility that Fedora itself provides for this task operates on one document at a time and is not librarian-friendly. A batch driven alternative is possible, but requires documents to be converted beforehand into the XML format used by the repository, necessitating a need for programming skills. In contrast, our new scheme allows arbitrary collections of documents residing on the user's computer (or the web at large) to be ingested into a Fedora repository in one operation, without a need for programming expertise. Provision is also made for editing existing documents and metadata, and adding new ones. The documents can be in a wide variety of different formats, and the user interface is suitable for practicing librarians. The design capitalizes on our experience in building the Greenstone librarian interface and participating in dozens of workshops with librarians worldwide.

text: A fedora librarian interface The Fedora content management system embodies a powerful and flexible digital object model. This paper describes a new open-source software front-end that enables end-user librarians to transfer documents and metadata in a variety of formats into a Fedora repository. The main graphical facility that Fedora itself provides for this task operates on one document at a time and is not librarian-friendly. A batch driven alternative is possible, but requires documents to be converted beforehand into the XML format used by the repository, necessitating a need for programming skills. In contrast, our new scheme allows arbitrary collections of documents residing on the user's computer (or the web at large) to be ingested into a Fedora repository in one operation, without a need for programming expertise. Provision is also made for editing existing documents and metadata, and adding new ones. The documents can be in a wide variety of different formats, and the user interface is suitable for practicing librarians. The design capitalizes on our experience in building the Greenstone librarian interface and participating in dozens of workshops with librarians worldwide.

year: 2008

title: Molecular dynamics decomposition of temperature-dependent elastic neutron scattering by a protein solution

authors: Hayward, Jennifer A.

abstract: Molecular dynamics simulations are performed of bovine pancreatic trypsin inhibitor in a cryosolution over a range of temperatures from 80 to 300 K and the origins identified of elastic dynamic neutron scattering from the solution. The elastic scattering and mean-square displacement calculated from the molecular dynamics trajectories are in reasonable agreement with experiments on a larger protein in the same solvent. The solvent and protein contributions to the scattering from the simulation model are determined. At lower temperatures (< 200 K) or on shorter timescales ( 10 ps) the scattering contributions are proportional to the isotopic nuclear scattering cross-sections of each component. However, for T > 200 K marked deviations from these cross-sections are seen due to differences in the dynamics of the components of the solution. Rapid activation of solvent diffusion leads to the variation with temperature of the total elastic intensity being determined largely by that of the solvent. At higher temperatures (>240 K) and longer times ( 100 ps) the protein makes the only significant contribution to the scattering, the solvent scattering having moved out of the accessible time-space window. Decomposition of the protein mean-square displacement shows that the observed dynamical transition in the solution at 200–220 K involves activation of both internal motions and external whole-molecule rotational and translational diffusion. The proportion that the external dynamics contributes to the protein mean-square displacement increases to  30 and 60% at 300 K on the 10- and 100-ps timescales, respectively.

text: Molecular dynamics decomposition of temperature-dependent elastic neutron scattering by a protein solution Molecular dynamics simulations are performed of bovine pancreatic trypsin inhibitor in a cryosolution over a range of temperatures from 80 to 300 K and the origins identified of elastic dynamic neutron scattering from the solution. The elastic scattering and mean-square displacement calculated from the molecular dynamics trajectories are in reasonable agreement with experiments on a larger protein in the same solvent. The solvent and protein contributions to the scattering from the simulation model are determined. At lower temperatures (< 200 K) or on shorter timescales ( 10 ps) the scattering contributions are proportional to the isotopic nuclear scattering cross-sections of each component. However, for T > 200 K marked deviations from these cross-sections are seen due to differences in the dynamics of the components of the solution. Rapid activation of solvent diffusion leads to the variation with temperature of the total elastic intensity being determined largely by that of the solvent. At higher temperatures (>240 K) and longer times ( 100 ps) the protein makes the only significant contribution to the scattering, the solvent scattering having moved out of the accessible time-space window. Decomposition of the protein mean-square displacement shows that the observed dynamical transition in the solution at 200–220 K involves activation of both internal motions and external whole-molecule rotational and translational diffusion. The proportion that the external dynamics contributes to the protein mean-square displacement increases to  30 and 60% at 300 K on the 10- and 100-ps timescales, respectively.

year: 2003-08

title: Te Kōtiritiri, Te Kōtaratara

authors: Maxwell, Te Kahautu

abstract: Haka. Lyrics composed by Te Kahautu Maxwell. Performed by Ōpōtiki Mai Tawhiti (Kapa Haka group) (3mins)

Waiata ā Tira: Aroha
Whakaeke: Pinepine Te Kura, Hau Te Kura
Mōteatea: Te Ao o Te Pārerā
Waiata ā Ringa: E pā to reo, Te Matatini, Herewini Parata
Poi: E ia e ia
Haka: Te Kōtiritiri, Te Kōtaratara
Whakawātea: Ōranga Tōiti, tōnui kōrero

text: Te Kōtiritiri, Te Kōtaratara Haka. Lyrics composed by Te Kahautu Maxwell. Performed by Ōpōtiki Mai Tawhiti (Kapa Haka group) (3mins)

Waiata ā Tira: Aroha
Whakaeke: Pinepine Te Kura, Hau Te Kura
Mōteatea: Te Ao o Te Pārerā
Waiata ā Ringa: E pā to reo, Te Matatini, Herewini Parata
Poi: E ia e ia
Haka: Te Kōtiritiri, Te Kōtaratara
Whakawātea: Ōranga Tōiti, tōnui kōrero

year: 2023-02-22