Moral Education in the Japanese Primary School Curricular Revision at the Turn of the Twenty-first Century: Aiming at a Rich and Beautiful Kokoro

This study examines values education in Japanese schools at the beginning of the millennium. The topic was approached by asking the following three questions concerning the curricular background, the morality conveyed through textbooks and the characterization of moral education from a comparative viewpoint: 1) What role did moral education play in the curriculum revision which was initiated in 1998 and implemented in 2002? 2) What kinds of moral responsibilities and moral autonomy do the moral texts develop? 3) What does Japanese moral education look like in terms of the comparative framework? The research was based on curriculum research. Its primary empirical data consisted of the national curriculum guidelines for primary school, which were taken into use in 2002, and moral texts, Kokoro no nôto, published by the Ministry of Education in the same context. Since moral education was approached in the education reform context, the secondary research material involved some key documents of the revision process from the mid-1990s to 2003. The research material was collected during three fieldwork periods in Japan (in 2002, 2003 and 2005). The text-analysis was conducted as a theory-dependent qualitative content analysis. Japanese moral education was analyzed as a product of its own cultural tradition and societal answer to the current educational challenges. In order to understand better its character, secular moral education was reflected upon from a comparative viewpoint. The theory chosen for the comparative framework, the value realistic theory of education, represented the European rational education tradition as well as the Christian tradition of values education. Moral education, which was the most important school subject at the beginning of modern school, was eliminated from the curriculum for political reasons in a school reform after the Second World War, but has gradually regained a stronger position since then. It was reinforced particularly at the turn of millennium, when a curriculum revision attempted to respond to educational and learning problems by emphasizing qualitative and value aspects. Although the number of moral lessons and their status as a non-official-subject remained unchanged, the Ministry of Education made efforts to improve moral education by new curricular emphases, new teaching material and additional in-service training possibilities for teachers. The content of the moral texts was summarized in terms of moral responsibility in four moral areas (intrapersonal, interpersonal, natural-supranatural and societal) as follows: 1) continuous self-development, 2) caring for others, 3) awe of life and forces beyond human power, and 4) societal contribution. There was a social-societal and emotional emphasis in what was taught. Moral autonomy, which was studied from the perspectives of rational, affective and individuality development, stressed independence in action through self-discipline and responsibility more than rational self-direction. Japanese moral education can be characterized as the education of kokoro (heart) and the development of character, which arises from virtue ethics. It aims to overcome egoistic individualism by reciprocal and interdependent moral responsibility based on responsible interconnectedness.

Stabilization of unusual structures in peptides using alpha,beta-dehydrophenylalanine: Crystal and solution structures of Boc-Pro-Delta Phe-Val-Delta Phe-Ala-OMe and Boc-Pro-Delta Phe-Gly-Delta Phe-Ala-OMe

The structures of two dehydropentapeptides, Boc-Pro-Delta Phe-Val-Delta Phe-Ala-OMe (I) and Boc-Pro-Delta Phe-Gly-Delta Phe-Ala-OMe (II) (Boc: t-butoxycarbonyl), have been determined by nuclear magnentic resonance (NMR), circular dichroism (CD), and X-ray, crystallographic studies. The peptide I assumes a S-shaped flat beta-bend structure, characterized by two partially overlapping type II beta-bends and absence of a second 1 <- 4 (N4-H center dot center dot center dot O1') intramolecular hydrogen bond. This is in contrast to the generally observed 3(10)-helical conformation in peptides with Delta Phe at alternate positions. This report describes the novel conformation assumed by peptide I and compares it with that of the conserved tip of the V3 loop of the HIV-1 envelope glycoprotein gp120 (sequence, G:P319 to F:P324, PDB code IACY). The tip of the V3 loop also assumes a S-shaped conformation with Arg:P322, making an intramolecular side-chain-backbone interaction with the carbonyl oxygen of Gly:P319. Interestingly, in peptide I, C(gamma)HVal(3) makes a similar side-chain-backbone C-H center dot center dot center dot O hydrogen bond with the carbonyl oxygen of the Boc group. The observed overall similarity indicates the possible use of the peptide as a viral antagonist or synthetic antigen. Peptide 11 adopts a unique turn followed by a 3(10)-helix. Both peptides I and II are classical examples of stabilization of unusual structures in oligopeptides.

Aqueous channels within apolar peptide aggregates. Solvated helix of Boc-Aib-Ala-Leu-Aib-Ala-Leu-Aib- -Ala-Leu-Aib-OMe. H2O.CH3OH

Although the peptide Boc-Aibl-Ala2-Leu3- Aib4-Alas Leu'-Aib7-Ala8-Leu9-Aib'0-OMe [with a t-butoxycarbonyl(Boc) blocking group at the amino terminus, a methyl ester (OMe) at the carboxyl terminus, and four a-aminoisobutyric (Aib) residues] has a 3-fold repeat of residues, the helix formed by the peptide backbone is irregular. The carboxyl-terminal half assumes an at-helical form with torsion angles ) and r of approximately -60° and -45°, respectively, whereas the amino-terminal half is distorted by an insertion of a water molecule between the amide nitrogen of Ala5 [N(5)] and the carbonyl oxygen of Ala2 [0(2)]. The water molecule W(1) acts as a bridge by forming hydrogen bonds N(5).W(1) (2.93 A) and W(1)---0(2) (2.86 A). The distortion of the helix exposes the carbonyl oxygens of Aib' and Aib4 to the outside environment, with the consequence that the helix assumes an amphiphilic character despite having all apolar residues. Neighboring helices in the crystal run in antiparallel directions. On one side of a helix there are only hydrophobic contacts with efficient interdigitation of leucine side chains with those from the neighboring helix. On the other side of the helix there are hydrogen bonds between protruding carbonyl oxygens and four water molecules that separate two neighboring helices. Along the helix axis the helices bind head-to-tail with a direct hydrogen bond N(2)-0(9) (3.00 A). Crystals grown from methanol/water solution are in space group P2, with a = 15.778 ± 0.004 A, b = 11.228 ± 0.002 A, c = 18.415 ± 0.003 A, = 102.10 ± 0.02ur and two formula units per cell for C49HON1003 2H2OCH3OH. The overall agreement factorR is 7.5% for 3394 reflections observed with intensities >3a(F), and the resolution is 0.90 A.

Differences in hydration and association of helical Boc-Val-Ala-Leu-Aib-Val-Ala-Leu-(Val-Ala-Leu-Aib)2-OMe. xH2O in two crystalline polymorphs

The 15-residue apolar peptide, Boc-Val-Ala-Leu-Aib-Val-Ala-Leu-(Val-Ala-Leu-Aib)h2a-sO Mebeen crystallized from 2-propanol-water (form I). The crystal parameters for I are as follows:C74H133N15018*2H20s,p ace group P21, a = 9.185 (6) A, b = 47.410 (3) A, c = 10.325 (9) A, @ = 91.47(2)O, 2 = 2, R = 6.3% for 4532 reflections observed >3aQ, resolution 0.94 A. The structure isalmost completely a-helical with eleven 5-1 hydrogen bonds and one 441 hydrogen bond nearthe N-terminus. The structure has been compared with a polymorph (form 11) obtained frommethanol-water (Karle, I. L.; Flippen-Anderson, J. L.; Uma, K.; Sukumar, M.; Balaram, P., J. An.Chem. SOC19. 90,112,9350-9356). The two forms differ in the extent of hydration; form I contains two water molecules in the head-to-tail region of helical columns, while form I1 is more extensively solvated, with the equivalent of 7.5 water molecules. The three-dimensional packing of helices is completely parallel in I and antiparallel in 11.

Domestic labour relations in India : Vulnerability and gendered life courses in Jaipur

This study explores labour relations between domestic workers and employers in India. It is based on interviews with both employers and workers, and ethnographically oriented field work in Jaipur, carried out in 2004-2007. Combining development studies with gender studies, labour studies, and childhood studies, it asks how labour relations between domestic workers and employers are formed in Jaipur, and how female domestic workers trajectories are created. Focusing on female part-time maids and live-in work arrangements, the study analyses children s work in the context of overall work force, not in isolation from it. Drawing on feminist Marxism, domestic labour relations are seen as an arena of struggle. The study takes an empirical approach, showing class through empiria and shows how paid domestic work is structured and stratified through intersecting hierarchies of class, caste, gender, age, ethnicity and religion. The importance of class in domestic labour relations is reiterated, but that of caste, so often downplayed by employers, is also emphasized. Domestic workers are crucial to the functioning of middle and upper middle class households, but their function is not just utilitarian. Through them working women and housewives are able to maintain purity and reproduce class disctinctions, both between poor and middle classes and lower and upper middle classes. Despite commodification of work relations, traditional elements of service relationships have been retained, particularly through maternalist practices such as gift giving, creating a peculiar blend of traditional and market practices. Whilst employers of part-time workers purchase services in a segmented market from a range of workers for specific, traditional live-in workers are also hired to serve employers round the clock. Employers and workers grudgingly acknowledged their dependence on one another, employers seeking various strategies to manage fear of servant crime, such as the hiring of children or not employing live-in workers in dual-earning households. Paid domestic work carries a heavy stigma and provide no entry to other jobs. It is transmitted from mothers to daughters and working girls were often the main income providers in their families. The diversity of working conditions is analysed through a continuum of vulnerability, generic live-in workers, particularly children and unmarried young women with no close family in Jaipur, being the most vulnerable and experienced part-time workers the least vulnerable. Whilst terms of employment are negotiated informally and individually, some informal standards regarding salary and days off existed for maids. However, employers maintain that workings conditions are a matter of individual, moral choice. Their reluctance to view their role as that of employers and the workers as their employees is one of the main stumbling blocks in the way of improved working conditions. Key words: paid domestic work, India, children s work, class, caste, gender, life course

Structure and conformation of the calcium complex of cyclo(Ala-Leu-Pro-Gly)2 in two crystal forms

Crystal structures of two different forms of the calcium perchlorate complex of cyclo(Ala-Leu-Pro-Gly)2 have been determined and refined using X-ray crystallographic techniques. Orthorhombic form: C32H52N8O8.Ca(ClO4)2.7H2O.2CH3OH, space group C222(1), a = 14.366, b = 18.653, c = 19.824 A, Z = 4, R = 0.068 for 2208 observed reflections. Monoclinic form: C32H52N8O8.Ca(ClO4)2.4H2O, space group C2, a = 21.096, b = 10.182, c = 11.256 A, beta = 103.33 degrees, Z = 2, R = 0.075 for 2165 observed reflections. The cyclic peptide molecule in both the structures has the form of a twofold symmetric, slightly elongated bowl. Type II' beta-turns, involving Gly and Ala at the corners, exist at the two ends of the molecule. The interior of the molecule is substantially hydrophilic, and the external surface of the bowl is largely hydrophobic. The calcium ion is located at the centre of the mouth of the bowl-like molecule. In both crystal forms, four peptide carbonyl oxygens from the cyclic peptide and two solvent oxygens coordinate to the metal ion. The mode of complexation may be described as incomplete encapsulation as, for example, in the case of metal complexes of antamanide. In the crystal structures the complex ions are held together by hydrogen bonds involving perchlorate ions and water molecules. The molecular structure observed in the crystals is entirely consistent with the results of solution studies, which also indicate the conformation of the cyclic peptide in the complex to be similar to that of the uncomplexed molecule.

Helix termination and chain reversal: Crystal and molecular structure of the alpha,beta-dehydrooctapeptide Boc-Val Delta Phe-Phe-Ala-Leu-Ala-Delta Phe-Leu-OH

The crystal structure of the dehydro octapeptide Boc-Val-Delta Phe-Phe-Ala-Leu-Ala-Delta Phe-Leu-OH has been determined to atomic resolution by X-ray crystallographic methods. The crystals grown by slow evaporation of peptide solution in methanol/water are orthorhombic, space group P2(1)2(1)2(1). The unit cell parameters are a = 8.404(3), b = 25.598(2) and c = 27.946(3) Angstrom, Z = 4. The agreement factor is R = 7.58% for 3636 reflections having (\F-o\) greater than or equal to 3 sigma (\F-o\). The peptide molecule is characterised by a 3(10)-helix at the N-terminus and a pi-turn at the C-terminus. This conformation is exactly similar to the helix termination features observed in proteins. The pi-turn conformation observed in the octapeptide is in good agreement with the conformational features of pi-turns seen in some proteins. The alpha(L)-position in the pi-turn of the octapeptide is occupied by Delta Phe(7), which shows that even bulky residues can be accommodated in this position of the pi-turns. In proteins, it is generally seen that alpha(L)-position is occupied by glycine residue. No intermolecular head-to-tail hydrogen bonds are observed in solid state structure of the octapeptide. A water molecule located in the unit cell of the peptide molecule is mainly used to hold the peptide molecule together in the crystal. The conformation observed for the octapeptide might be useful to understand the helix termination and chain reversal in proteins and to construct helix terminators for denovo protein design.

Observation of Water-Mediated Helix-Terminating Conformation in a Dehydrophenylalanine Peptide: Crystal and Solution Structure of the Octapeptide Ac-.DELTA.Phe-Val-.DELTA.Phe-Phe-Ala-Val-.DELTA.Phe-Gly-OMe

We have synthesised and determined the solution conformation and X-ray crystal structure of the octapeptide Ac-Delta Phe(1)-Val(2)-Delta Phe(3)-Phe(4)-Ala(5)-Val(6)-Delta Phe(7)-Gly(8)-OCH3 (Delta Phe = alpha,beta-dehydrophenylalanine) containing three Delta Phe residues as conformation constraining residues. In the solid state, the peptide folds into (i) an N-terminal (3)10(R)-helical pentapeptide segment, (ii) a middle non-helical segment, and (iii) a C-terminal incipient (3)10(L)-helical segment. The results of H-1 NMR data also suggest that a similar multiple-turn conformation for the peptide is largely maintained in solution. Though the C-terminal helix is incipient, the overall conformation of the octapeptide matches well with the conformation of the hairpins reported. Comparison of the pi-turn seen in the octapeptide molecule with those observed in proteins at the C-terminal end of helixes shows the structural similarity among them. A water molecule mediates the 5 --> 2 hydrogen bond in the pi-turn region. This is the first example of a water-inserted pi-turn in oligopeptides reported so far. Comparison between the present octapeptide and another (3)10(R)-helical dehydro nonapeptide Boc-Val-Delta Phe-Phe-Ala-Phe-Delta Phe-Val-Delta Phe-Gly-OCH3 solved by us recently, demonstrates the possible sequence-dependent conformational variations in alpha,beta-dehydrophenylalanine-containing oligopeptides.

Role of two consecutive alpha,beta-dehydrophenylalanines in peptide structure: Crystal and molecular structure of Boc-Leu-Delta Phe-Delta Phe-Ala-Phe-NHMe

An N-alpha-protected model pentapeptide containing two consecutive Delta Phe residues, Boc-Leu-Delta Phe-Delta Phe-Ala-Phe-NHMe, has been synthesized by solution methods and fully characterized. H-1-nmr studies provided evidence for the occurrence of a significant population of a conformer having three consecutive, intramolecularly II-bonded beta-bends in solution. The solid state structure has been determined by x-ray diffraction methods. The crystals grown from aqueous methanol are orthorhombic, space group P2(1)2(1)2(1),, a = 11.503(2), b = 16.554(2), c = 22.107(3) Angstrom, V = 4209(1) Angstrom,(3) and Z = 4. The x-ray data were collected on a CAD4 diffractometer using CuKalpha radiation (lambda = 1.5418 Angstrom). The structure was determined using direct methods and refined by full-matrix least-squares procedure. The R factor is 5.3%. The molecule is characterized by a right handed 3(10)-helical conformation ((phi) = -68.2 degrees (psi) = -26.3 degrees), which is made up of two consecutive type III beta-bends and one type I beta-bend. In the solid state the helical molecules are aligned head-to-tail, thus forming long rod like structures. A comparison with other peptide structures containing consecutive Delta Phe residues is also provided. The present study confirms that the -Delta Phe-Delta Phe-sequence can be accommodated in helical structures. (C) 1997 John Wiley & Sons, Inc.

Chain Length Effects on Helix-Hairpin Distribution in Short Peptides with Aib-(D)Ala and Aib-Aib Segments

The Aib-(D)Ala dipeptide segment has a tendency to form both type-I'/III' and type-I/III beta-turns. The occurrence of prime turns facilitates the formation of beta-hairpin conformations, while type-I/III turns can nucleate helix formation. The octapeptide Boc-Leu-Phe-Val-Aib-(D)Ala-Leu-Phe-Val-OMe (1) has been previously shown to form a beta-hairpin in the crystalline state and in solution. The effects of sequence truncation have been examined using the model peptides Boc-Phe-Val-Aib-Xxx-Leu-Phe-NHMe (2, 6), Boc-Val-Aib-Xxx-Leu-NHMe (3, 7), and Boc-Aib-Xxx-NHMe (4, 8), where Xxx = (D)Ala, Aib. For peptides with central Aib-Aib segments, Boc-Phe-Val-Aib-Aib-Leu-Phe-NHMe (6), Boc-Val-Aib-Aib-Leu-NHMe (7), and Boc-Aib-Aib-NHMe (8) helical conformations have been established by NMR studies in both hydrogen bonding (CD(3)OH) and non-hydrogen bonding (CDCl(3)) solvents. In contrast, the corresponding hexapeptide Boc-Phe-Val-Aib-(D)Ala-Leu-Phe-Val-NHMe (2) favors helical conformations in CDCl(3) and beta-hairpin conformations in CD(3)OH. The beta-turn conformations (type-I'/III) stabilized by intramolecular 4 -> 1 hydrogen bonds are observed for the peptide Boc-Aib-(D)Ala-NHMe (4) and Boc-Aib-Aib-NIiMe (8) in crystals. The tetrapeptide Boc-Val-Aib-Aib-Leu-NHMe (7) adopts an incipient 3(10)-helical conformation stabilized by three 4 -> 1 hydrogen bonds. The peptide Boc-Val-Aib-(D)Ala-Leu-NHMe (3) adopts a novel et-turn conformation, stabilized by three intramolecular hydrogen bonds (two 4 -> 1 and one 5 -> 1). The Aib-L(D)Ala segment adopts a type-I' beta-turn conformation. The observation of an NOE between Val (1) NH <-> HNCH(3) (5) in CD(3)OH suggests, that the solid state conformation is maintained in methanol solutions. (C) 2011 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 96: 744-756, 2011.

La ley nueva y la nueva evangelización : la tradición tomista y la perspectiva moral de Evangelii gaudium

Resumen: Las indicaciones pastorales del Papa Francisco en Evangelii gaudium ofrecen la oportunidad para redescubrir el valor de la categoría ley bajo la guía de la tradición tomista recogida en el documento pontificio. La propuesta moral del Evangelio o ley nueva, siguiendo la sinonimia utilizada por santo Tomás de Aquino, no puede ser reducida a un precepto o una serie de normas; muy por el contrario, revisitando la doctrina del Doctor Común podemos descubrir la necesidad de una hermenéutica sapiencial y profundamente bíblica de uno de los pilares de la moral cristiana. En el camino de la conversión pastoral, el retorno a las fuentes tomistas vuelve a iluminar la reflexión teológica con fecundidad renovada.

La ley moral natural y ley positiva humana en el opúsculo “La filosofía jurídica del artículo 19 de la Constitución Nacional”, de Arturo Enrique Sampay

La Constitución Nacional reconoce un orden de conducta instituido por Dios y otro instituido por el Estado… el débito legal debe resultar conforme al débito moral. Si así no fuera, cualquier imposición del legislador no sería derecho sino un acto de violencia desnaturalizando el poder que el Estado tiene de reforzar con débito eventualmente coercible obligaciones emergentes de la virtud de la justicia. En este trabajo nos ocuparemos de la relación entre ley moral natural y la ley positiva humana a partir de las consideraciones que Arturo Enrique Sampay2 formula en su obra, La filosofía jurídica del Artículo 19 de la Constitución Nacional3. Sampay desarrolla el tópico principalmente con la inspiración de la doctrina de Tomás de Aquino.

La literatura jurídica como praxis moral

Resumen: La dimensión literaria del acto comunicacional científico-jurídico es un elemento implícito en la interacción de la retórica y dialéctica jurídicas. La matriz artística surge ya del parangón ofrecido por Aristóteles en la Retórica: la evocación de la antistrofa (figura que nos reenvía a pulso cierto al arte poético) lo dice todo, apenas sugiriendo. La comunicación que defenderemos consiste en afirmar que la belleza del acto comunicacional científico jurídico y la perfección de su arte son imputables a su autor y supone una responsabilidad de tipo moral que trasunta en el arte comunicativo el vaso de lo comunicado. Existe una lealtad del recipiente al contenido implícita en la metáfora aristotélica, que requiere una fidelidad del científico para dar cuenta del tesoro que lleva en sus vasijas endebles.