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  • 1
    Online Resource
    Online Resource
    Geo-intelligence for Sustainable Development (2021)
    Singapore :Springer Nature Singapore :
    Details
    Keywords: Sustainability. ; Geography. ; Geographic information systems. ; Quantitative research. ; Climatology. ; Natural disasters. ; Sustainability. ; Regional Geography. ; Geographical Information System. ; Data Analysis and Big Data. ; Climate Sciences. ; Natural Hazards.
    Description / Table of Contents: Geo-intelligence role in sustainable city missions of the global south: a review -- Cloud-based geospatial mapping and analysis of prayagraj kumbh mela of india: the unesco intangible cultural heritage -- Geo-intelligence-based approach for sustainable development of peri-urban areas: a case study of kozhikode city, kerala (india) -- Smart city: artificial intelligence in the city of the future -- Geo-intelligence for ecosystem services in poverty alleviation and food security -- Geo-intelligence for pandemic prevention and control -- Geo- intelligence in public health: a panoptical to covid -19 pandemic -- Use of remote sensing data to identify air pollution signatures in india -- Urban growth impact on cauvery river: a geospatial perspective -- Artificial neural network (ann) based predictions of bulk permittivity of co2-water-porous media system -- Long-term satellite data time series analysis for land degradation mapping to support sustainable land management in ukraine -- Modeling of the mass balance of glaciers with debris cover -- A geo-intelligence based approach to investigate temporal changes in the length and surface area and ice velocity of sakchum glacier. .
    Abstract: Globally, concerns for the environment and human well-being have increased as results of threats imposed by climate change and disasters, environmental degradation, pollution of natural resources, water scarcity and proliferation of slums. Finding appropriate solutions to these threats and challenges is not simple, as these are generally complex and require state-of-the-art technology to collect, measure, handle and analyse large volumes of varying data sets. However, the recent advances in sensor technology, coupled with the rapid development of computational power, have greatly enhanced our abilities to capture, store and analyse the surrounding physical environment. This book explores diverse dimensions of geo-intelligence (GI) technology in developing a computing framework for location-based, data-integrating earth observation and predictive modelling to address these issues at all levels and scales. The book provides insight into the applications of GI technology in several fields of spatial and social sciences and attempts to bridge the gap between them.
    Type of Medium: Online Resource
    Pages: XV, 227 p. 101 illus., 92 illus. in color. , online resource.
    Edition: 1st ed. 2021.
    ISBN: 9789811647680
    Series Statement: Advances in Geographical and Environmental Sciences,
    URL: https://doi.org/10.1007/978-981-16-4768-0
    DOI: 10.1007/978-981-16-4768-0
    DDC: 304.2
    Language: English
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  • 2
    Monograph available for loan
    Monograph available for loan
    Geoinformatics for climate change studies (2011)
    New Delhi : TERI Press
    Details Availability
    Call number: PIK L 031-13-0018
    Description / Table of Contents: Contents: 1 A GIS-based framework for modeling and global design of Earth systems ; 2 Geoinformatics for climate change research ; 3 Reactions of mountain glaciers to climate change - a remote sensing approach ; 4 Geoinformatics and the mapping of Lands vulnerable to sea level rise ; 5 Geospatial tools to assess forest ecosystems under climate change trajectories ; 6 Geoinformatics for comprehensive impact assessment and analysis of climate change for integrated water resources management ; 7 Climate - Population - Energy: Prognoses for 2050 ; 8 Geoprocessing for soft mapping of sparse and inaccurate evapotranspiration data ; 9 Impact of climate variability on human health ; 10 Geo-information-based approach for monitoring climate-induced land degradation in Nigeria ; 11 Assessing Land surface temperature over Bangladesh using MODIS satellite images - an indicator of climate change ; 12 High resolution climate change scenarios for Morocco for the 21st century ; 13 GIScience tools for climate change related natural hazards and modeling ; 14 Spatial data infrastructure convergence: Building SDI bridges to address climate change ; 15 Geoinformatics for Climate Change Adaptation and Disaster Risk Reduction ; 16 Geoinformatics and communication technologies for climate change hazards: Musing beyond the technical issues
    Type of Medium: Monograph available for loan
    Pages: XVIII, 470 S. : Ill., graph. Darst., Kt.
    ISBN: 9788179934098
    Location: A 18 - must be ordered
    Branch Library: PIK Library
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  • 3
    Electronic Resource
    Electronic Resource
    Modulation of phospholipase A2 activity generated by molecular evolution (1999)
    Springer
    Cellular and molecular life sciences 56 (1999), S. 384-397 
    Details
    ISSN: 1420-9071
    Keywords: Key words. Phospholipase A2; molecular evolution;inhibitor; pharmacological sites; enzyme activity; enzyme toxicity.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Snake venom oligomeric neurotoxins offer several unique examples of modulation of phospholipase A2 (PLA2) activity generated by molecular evolution. This phenomenon was found in evolutionary younger snakes and is probably common for representatives of the genus Vipera. At present, the best-studied example is the heterodimeric neurotoxin vipoxin from the venom of the southeast European snake Vipera ammodytes meridionalis. It is a complex between a basic strongly toxic PLA2 and an acidic and catalytically inactive PLA2-like component (Inh). This is the first reported example of a high degree of structural homology (62%) between an enzyme and its natural protein inhibitor. The inhibitor is a product of the divergent evolution of the unstable PLA2 in order to stabilize it and to preserve the pharmacological activity/toxicity for a long time. Inh reduces both the catalytic activity and toxicity of PLA2. Vipoxin also illustrates evolution of the catalytic into a inhibitory function. Vipoxin analogues have been found in the venom of viperid snakes inhabiting diverse regions of the world. An attempt is made to explain modulation of the toxic function by the three-dimensional structure of vipoxin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000180050440
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  • 4
    Electronic Resource
    Electronic Resource
    Structure of the bifunctional inhibitor of trypsin and α-amylase from ragi seeds at 2.9 Å resolution (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 25-30 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structure of a bifunctional inhibitor of α-amylase and trypsin from the seeds of ragi (Indian finger millet, Eleusine coracana Gaertneri) has been determined by an X-ray diffraction method. The inhibitor consists of 122 amino acids with five disulfide bridges and belongs to the plant α-amylase/trypsin-inhibitor family. This is the first crystal structure determination of a member of this family. The protein, purified from the seeds of ragi, has a molecular mass of 13300 Da with a pI of 10.3. Crystals were grown by a microdialysis method using ammonium sulfate as precipitant. The improved purification protocol and the modified crystallization conditions enabled reproducible growth of the crystals. The cell parameters are a = 41.2, b = 47.4, c = 55.9 Å. The intensity data were collected to 2.9 Å resolution, and the crystal structure was determined using the molecular-replacement method. The structure was refined using the X-PLOR and CCP4 program packages to a conventional R factor of 21%. The structure contains four α-helices between residues 19–29, 37–51, 56–65 and 90–95, and two short antiparallel β-strands between residues 67–70 and 73–75.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444998006271
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  • 5
    Electronic Resource
    Electronic Resource
    A novel 40 kDa protein from goat mammary secretions: purification, crystallization and preliminary X-ray diffraction studies (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1332-1333 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A novel 40 kDa protein has been purified from dry secretions of the mammary gland of goats. The first 15 N-terminal residues were sequenced and showed a sequence identity of 30% to a novel 39 kDa whey protein from bovine mammary secretions. The protein was crystallized by the microdialysis method. Protein was dissolved to a concentration of 40 mg ml−1 in 0.025 M Tris–HCl pH 8.0 and equilibrated with the same buffer containing 19%(v/v) ethanol. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 66.1, b = 107.8, c = 63.2 Å and one molecule per asymmetric unit. Intensity data were collected to 2.9 Å resolution, with a completeness of 95%. Since no similar model is available in the protein structure database, heavy-atom derivatives have been prepared and three-dimensional structure determination using the isomorphous replacement method is in progress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901012070
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  • 6
    Electronic Resource
    Electronic Resource
    Purification, crystallization and preliminary X-ray crystallographic analysis of lactoperoxidase from buffalo milk (1995)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 1094-1096 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The lactoperoxidase was prepared from buffalo milk and purified using CM-Sephadex C-50 and Sephadex G-100. The activity of the enzyme was measured using 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) diammonium salt as a chromogenic substrate at pH 6.0. The purified protein was crystallized from 0.01 M sodium phosphate buffer (pH 8.0) with 10%(v/v) ethanol by the sitting-drop vapour-diffusion method. The green-coloured plate-like crystals are orthorhombic in space group P212121 with unit-cell dimensions a = 116.9, b = 103.2 and c = 62.3 Å. The asymmetric unit contains one molecule with a solvent content of 52%. The crystals were stable in the X-ray beam and diffract beyond 3.2 Å. The native data to 3.5 Å have been collected and the structure determination is in progress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444995004422
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  • 7
    Electronic Resource
    Electronic Resource
    Purification, crystallization and preliminary crystallographic analysis of mare lactoferrin (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 1196-1198 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Lactoferrin is an iron-binding glycoprotein with a molecular weight of 80 kDa. The protein has two iron binding sites. It has two structural lobes, each housing one Fe3+ and the synergistic CO32− ion. The protein was isolated from the colostrum/milk of mares maintained at National Research Centre on Equines, Hisar, India. The purified samples of the protein were crystallized using a microdialysis method. The protein was dialysed against low ionic strength buffer solution. Several crystal forms were obtained, out of which three were characterized which have cell dimensions as follows. Form I a = 79.8, b = 103.5, c = 112.0 Å, space group P212121, with one protein molecule per asymmetric unit and a solvent content of 57%. Form II a = 84.9, b = 99.7, c = 103.5 Å, space group P212121 with one molecule per asymmetric unit and a solvent content of 55%. Form III a = 151.0, b = 151.0, c = 240.6 Å, space group P41212 with three molecules in the asymmetric unit and a solvent content of 57%. The intensity data up to 3.8 Å resolution for form I, 2.9 Å resolution data for form II and 6 Å resolution data for form III have been collected. Further calculations are in progress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996007986
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  • 8
    Electronic Resource
    Electronic Resource
    Purification, crystallization and preliminary crystallographic analysis of a natural complex of phospholipase A2 from Echis carinatus (saw-scaled viper) (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 1240-1241 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A novel complex of phospholipase A2 complexed with another venom protein has been isolated and purified from saw-scaled viper (Echis carinatus) venom. The molecular weights of the two components are 16 and 14 kDa, respectively. The complex was purified using an Affigel blue column and an anion-exchange (DEAE Sephacel) column. Long diamond-shaped crystals were obtained by hanging-drop vapour diffusion. The protein complex was dissolved at a concentration of 10 mg ml−1 in 20 mM sodium cacodylate, 1 mM CaCl2 and 2% dioxane at pH 6.0. The reservoir contained the same buffer with 7%(w/v) PEG 4000. Crystals appeared within 2–3 weeks. Native data to 2.9 Å resolution have been obtained at 291 K. The crystals belong to the monoclinic space group P21 with unit-cell parameters a = 74.47, b = 47.87, c = 106.39 Å, β = 104.5° and contain two molecules per asymmetric unit. Structure determination by molecular replacement is in progress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999004783
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  • 9
    Electronic Resource
    Electronic Resource
    Purification, crystallization and preliminary X-ray crystallographic analysis of a phospholipase A2 from Daboia russelli pulchella (1999)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 925-926 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Phospholipases are esterolytic enzymes which hydrolyze glycerophospholipids. The pharmacological efficiency of phospholipase A2 (PLA2) enzymes is reflected by their specificity towards a tissue or organ. The Russell's viper has been classified into two classes. Class 1 contains Viper russelli russelli, Viper russelli siamensis and Viper russelli formosensis, whereas class 2 contains Daboia russelli pulchella. The sequence identity between the PLA2s from these two classes is 47%. The novel PLA2 from Daboia russelli pulchella has been crystallized using the hanging-drop vapour-diffusion method with ammonium sulfate as precipitating agent. Crystals belong to the orthorhombic space group C2221 with unit-cell parameters a = 77.01, b = 92.29, c = 76.90 Å and two molecules in the asymmetric unit. These crystals diffract to about 2.49 Å resolution using a rotating-anode source.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S090744499900058X
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  • 10
    Electronic Resource
    Electronic Resource
    Structure of buffalo lactoferrin at 3.3 Å resolution at 277 K (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 684-689 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The three-dimensional structure of diferric buffalo lactoferrin has been determined at 3.3 Å resolution. The structure was solved by molecular replacement using the coordinates of diferric human lactoferrin as a search model and was refined by simulated annealing (X-PLOR). The final model comprises 5316 protein atoms for all 689 residues, two Fe3+ and two CO_{3}^{2-} ions. The final R factor was 21.8% for 11 711 reflections in the resolution range 17.0–3.3 Å. The folding of buffalo lactoferrin is essentially similar to that of the other members of the transferrin family. The significant differences are found in the dimensions of the binding cleft and the interlobe orientation. The interlobe interactions are predominantly hydrophobic in nature, thus facilitating the sliding of two lobes owing to external forces. The interdomain interactions are comparable in the N and C lobes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900005151
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