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Dynamics of Development Communication: Awareness, Motivation, Participation
A critique from a communication perspective focuses on reciprocal relations among patterns of Interaction and the social realities of various agents. In development programs in India, the agents include government bureaucracy and the masses. The critique is based on three sets of information: 1) a review of international communication providing an international perspective on Indian development programs; 2) a review of Indian development programs and development communication in India focusing on the development activities, reasons behind these activities and the conventional wisdom about the effects of these programs; and 3) a study of development participation effectiveness in a rural and rurban community. The study describes the patterns of communication about various development projects, relationships among communication patterns; forms of participation in development programs, cognitive/attitudinal variables (awareness, discontent, motivation, etc.), and the adoption of various development objectives. Results suggest startling conclusions: existing patterns of communication and the people\u27s perception of government pose a major impediment to continued development. Development programs are well received by the people and are effective but produce dependence. The social environments of the poor exacerbate this effect, and the ineffective development delivery system heightens discontent. To intercept this spiral of discontent/dependency, the government has relied on mass media and government agents. The data indicates that these are the least effective means of communication, but perhaps the best available, given the social structure of the two coraiiiunities. The one-way mass media model has only information-generation function whereas the two-way interpersonal model does not urge people for participation. A different communication handling is needed for conurbation communities and women as compared to rural and men. The dysfunctional effects of development communication suggest a poor communication dialogue
Crystal and molecular structure of the doubly unsaturated dehydropeptide Ac-ΔPhe-Ala-ΔPhe-NH-Me
The dehydropeptide Ac-ΔPhe-L-Ala-ΔPhe-NH-Me, containing two dehydro-phenylalanine (ΔPhe) residues, crystallizes from methanol/water in space group P212121, with a = 12.508 (2), b = 12.746(1) and c = 15.465(9).
In the crystalline state, the peptide chain assumes a right-handed 310-helical conformation stabilized by two intramolecular hydrogen bonds, between the N-terminal acetyl group and the NH of ΔPhe3, and between the CO of ΔPhe1 and the NH of the C-terminal methylamide group, respectively. The two consecutive 10-membered rings formed by the hydrogen bonds have torsion angles quite close to the standard values for type III β-bends. ΔPhe1 is located in the (i + 1) position of the first β-bend, while ΔPhe2 is located in the (i + 2) position of the other β-bend.
In the crystal, the molecules are linked head to tail by intermolecular hydrogen bonds to form long helical chains. The axes of the helices are parallel to the c axis, but neighboring helices run in antiparallel directions. This crystal packing is similar to the packing motifs frequently observed in Aib-containing peptides
Crystal and molecular structure of the doubly unsaturated dehydropeptide Ac-?Phe-Ala-?Phe-NH-Me
Crystal and molecular structure of Boc-D-Ala-?Phe-Gly-?Phe-D-Ala-OMe: A 310-helical dehydropeptide
Crystal and molecular structure of Boc-D-Ala-ΔPhe-Gly-ΔPhe-D-Ala-OMe: A 310-helical dehydropeptide
The crystal and molecular structure of the pentapeptide Boc-D-Ala-ΔPhe-Gly-ΔPhe-D-Ala-OMe, containing two dehydrophenylalanine residues, was determined by x-ray diffraction. The molecule crystallizes in the orthorombic P212121 space group, with a = 10.439(3), b = 15.319(3) and c = 21.099(4) Å. In the solid state, the conformation of the pentapeptide is characterized by the presence of two type III′ β-turns. Thus the peptide assumes a left-handed 310-helical conformation, the left sense being due to the D configuration of the alanine residues. The two unsaturated residues are located in the (i + 1) position of the first β-turn and in the (i + 2) position of the second β-turn, respectively. In the crystal, the helical molecules are linked head to tail by hydrogen bonds. Lateral hydrogen bonds are also formed between molecules related by a twofold screw symmetry. This gives rise to a typical mode of packing characterized by infinite helical “chains,” smiliar to the packing found in other oligopeptides that adopt a 310-helical structure