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  • Protein-nucleic acid interaction  (2)
  • Kerala  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Traditional homegardens of Kerala: a sustainable human ecosystem (1993)
    Springer
    Agroforestry systems 24 (1993), S. 203-213 
    Details
    ISSN: 1572-9680
    Keywords: Kerala ; homegardens ; agroforestry ; low input agriculture ; sustainability ; architectural analysis ; human ecosystem
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract An analogue approach to analysing the traditional homegardens of Keralavis-à-vis natural climax ecosystems is adopted. The traditional homegarden is apparently a climax ecosystem, where ecological succession is consciously manipulated by human beings. High intensity of vertical and horizontal space use, the highly dynamic chronological structure and the capacity to perform essential ecological processes make this ecosystem relatively sustainable. Homegardens in Kerala effectively serve as human ecosystems with their low input demand, staggered supply of outputs, and enhancement of habitat quality. However, recent trends in agrarian structure and the high market orientation exert pressures on the homegarden, and its sustainability as a human ecosystem is in question.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00706892
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    Paper (German National Licenses)
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  • 2
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    Mapping the interactions of the single-stranded DNA binding protein of bacteriophage T4 (gp32) with DNA lattices at single nucleotide resolution: polynucleotide binding and cooperativity (2015)
    Oxford University Press
    Details
    Publication Date: 2015-10-31
    Description: We here use our site-specific base analog mapping approach to study the interactions and binding equilibria of cooperatively-bound clusters of the single-stranded DNA binding protein (gp32) of the T4 DNA replication complex with longer ssDNA (and dsDNA) lattices. We show that in cooperatively bound clusters the binding free energy appears to be equi-partitioned between the gp32 monomers of the cluster, so that all bind to the ssDNA lattice with comparable affinity, but also that the outer domains of the gp32 monomers at the ends of the cluster can fluctuate on and off the lattice and that the clusters of gp32 monomers can slide along the ssDNA. We also show that at very low binding densities gp32 monomers bind to the ssDNA lattice at random, but that cooperatively bound gp32 clusters bind preferentially at the 5'-end of the ssDNA lattice. We use these results and the gp32 monomer-binding results of the companion paper to propose a detailed model for how gp32 might bind to and interact with ssDNA lattices in its various binding modes, and also consider how these clusters might interact with other components of the T4 DNA replication complex.
    Keywords: Protein-nucleic acid interaction
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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  • 3
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    Mapping the interactions of the single-stranded DNA binding protein of bacteriophage T4 (gp32) with DNA lattices at single nucleotide resolution: gp32 monomer binding (2015)
    Oxford University Press
    Details
    Publication Date: 2015-10-31
    Description: Combining biophysical measurements on T4 bacteriophage replication complexes with detailed structural information can illuminate the molecular mechanisms of these ‘macromolecular machines’. Here we use the low energy circular dichroism (CD) and fluorescent properties of site-specifically introduced base analogues to map and quantify the equilibrium binding interactions of short (8 nts) ssDNA oligomers with gp32 monomers at single nucleotide resolution. We show that single gp32 molecules interact most directly and specifically near the 3'-end of these ssDNA oligomers, thus defining the polarity of gp32 binding with respect to the ssDNA lattice, and that only 2–3 nts are directly involved in this tight binding interaction. The loss of exciton coupling in the CD spectra of dimer 2-AP (2-aminopurine) probes at various positions in the ssDNA constructs, together with increases in fluorescence intensity, suggest that gp32 binding directly extends the sugar-phosphate backbone of this ssDNA oligomer, particularly at the 3'-end and facilitates base unstacking along the entire 8-mer lattice. These results provide a model (and ‘DNA map’) for the isolated gp32 binding to ssDNA targets, which serves as the nucleation step for the cooperative binding that occurs at transiently exposed ssDNA sequences within the functioning T4 DNA replication complex.
    Keywords: Protein-nucleic acid interaction
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
    Published by Oxford University Press
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