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  • 1
    Electronic Resource
    Electronic Resource
    A brand share prediction model based on several disparate sources of data: an empirical model of detergent choice in Mumbai, India (2004)
    [S.l.] : Emerald
    Asia Pacific journal of marketing and logistics 16 (2004), S. 3-22 
    Details
    ISSN: 1355-5855
    Source: Emerald Fulltext Archive Database 1994-2005
    Topics: Economics
    Notes: We describe the application of a nested logit function for modelling consumer brand choice using household transaction data from the Indian market. This is unique since it is one of the first attempts to integrate disparate consumer information sources available at various levels of aggregation towards developing a prediction model for brand market share in India. We test the usefulness of the model for forecasting brand market share in the premium detergents market in Mumbai, India. The results of the model building exercise reveal the importance of advertising, specifically the role of ad message in influencing brand choice. It is concluded that such modelling initiatives show significant returns for market planning exercises in developing markets. However, the need for streamlining the collection of market data and its subsequent organization in a form that can help develop more portent prediction models is apparent.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1108/13555850410765203
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  • 2
    Electronic Resource
    Electronic Resource
    Store choice behaviour in an evolving market (2004)
    Bingley : Emerald
    International journal of retail and distribution management 32 (2004), S. 482-494 
    Details
    ISSN: 0959-0552
    Source: Emerald Fulltext Archive Database 1994-2005
    Topics: Economics
    Notes: The objective of this study is to identify, at a macro level, the drivers of store choice in various product categories, in the context of the evolving retail industry in India. The paper attempts to correlate the distinct store features as perceived by respondents with the true motivations of various consumers in patronising various stores. In the process it provides insight as to whether the average Indian consumer values the new store dimensions offered by retailers as a part of the new formats emerging in the market place. The framework evolved for evaluating effectiveness of newer store formats is necessary since it has a major impact on the overall profitability of the retailing business. Suggests that customers in a developing market such as India do not require the service paraphernalia offered by many of the new store formats emerging in the market and notes that this may cast a serious doubt over the retail revolution, which has taken shape in the Indian markets lately. Some hypotheses about the evolution of the retailing business in India, which requires further investigation, are suggested.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1108/09590550410558626
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  • 3
    Electronic Resource
    Electronic Resource
    tert-Butyl N-{2-[N-(N,N′-dicyclohexylureidocarbonylethyl)carbamoyl]prop-2-yl}carbamate (2000)
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 1120-1121 
    Details
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The title compound, C25H44N4O5, exhibits a turn with the main chain reversing direction, held together by an intramolecular N—H...O hydrogen bond. In the urea fragment, a notable amide C—N bond between the carboxyl C and the tertiary N atom shows marked single-bond character [1.437 (2) Å]. The dihedral angle of the β-alanyl residue, centrally located in the turn, is gauche [69.2 (2)°]. The packing is mediated by two intermolecular hydrogen bonds and van der Waals contacts involving the methyl moieties and the cyclohexyl rings.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108270100007447
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  • 4
    Electronic Resource
    Electronic Resource
    Solid state and solution conformations of a helical peptide with a central gly-gly segment (1996)
    New York : Wiley-Blackwell
    Biopolymers 38 (1996), S. 515-526 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The influence of amino acids with contrasting conformational tendencies on the stereochemistry of oligopeptides has been investigated using an octapeptide Boc-Leu-Aib-Val-Gly-Gly-Leu-Aib-Val-OMe, which contains two helix-promoting Aib residues and a central helix-destabilizing Gly-Gly segment. Single crystal x-ray diffraction studies reveal that a 3 10-helix is formed up to the penultimate Aib residue, at which point there is a helix reversal in the backbone, reminiscent of a C-terminal 6 → I hydrogen bond. The curious feature in the crystal is the solvation of the possible 6 → 1 bond by a CH3OH molecule, where the OH is inserted between O(3) and N(8) and participates in hydrogen bonds with both. The cell parameters are as follows: space group P212121, a = 10.649(4) Å, b = 15.694(5) Å, c = 30.181(8) Å, R = 6.7% for 3427 data (| F0| 〉 3σF) observed to 0.9 Å. Nuclear magnetic resonance studies in CDCl3 using NH group solvent accessibility and nuclear Overhauser effects as probes are consistent with a 3 10-helical conformation. In contrast, in (CD3)2SO, unfolding of the central segment results in a multiple β-turn structure, with β-turn conformations populated at residues 1-2, 3-4, and 6-7. CD studies in methanol-2,2,2-trifluoroethanol (TFE) mixtures also provide evidence for a solvent-dependent structural transition. Helical conformations are populated in TFE, while type II β-turn structures are favored in methanol. © 1996 John Wiley & Sons, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Omega amino acids in peptide design: incorporation into helices (1996)
    New York : Wiley-Blackwell
    Biopolymers 39 (1996), S. 769-777 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Incorporation of easily available achiral ω-amino acid residues into an oligopeptide results in substitution of amide bonds by polymethylene units of an aliphatic chain, thereby providing a convenient strategy for constructing a peptidomimetic. The central Gly-Gly segment of the helical octapeptide Boc-Leu-Aib-Val-Gly-Gly-Leu-Aib-Val-Ome(1) has been replaced by δ-amino-valeric acid (δ-Ava) residue in the newly designed peptide Boc-Leu-Aib-Val-δ-Ava-Leu-Aib-Val-OMe(2). 1H-nmr results clearly suggest that in the apolar solvent CDCl3, the δ-Ava residue is accommodated into a folded helical conformation, stabilized by successive hydrogen bonds involving the NH groups of Val(3), δ-Ava(4), and Leu(5). The δ-Ava residue must adopt a gauche-gauche-trans-gauche-gauche conformation along the central polymethylene unit of the aliphatic segment, a feature seen in an energy-minimized model conformation based on nmr parameters. The absence of hydrogen bonding functionalities, however, limits the elongation of the helix. In fact, in CDCl3, the folded conformation consists of an N-terminal helix spanning residues 1-4, followed by a Type II β-turn at residues 5 and 6, whereas in strongly solvating media like (CD3)2SO, the unfolding of the N-terminal helix results in β-turn conformations at Leu(1)-Aib(2). The Type II β-turn at the Leu(5)-Aib(6) segment remains intact even in (CD3)2SO. CD comparisons of peptides 1 and 2 reveal a “nonhelical” spectrum for 2 in 2,2,2-trifluoroethanol. © 1996 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    5-Membered NH…N hydrogen bonded molecular scaffold in a model dipeptide containing 3-aminophenylacetic acid: Crystal and solution conformations (2000)
    Springer
    International journal of peptide research and therapeutics 7 (2000), S. 353-358 
    Details
    ISSN: 1573-3904
    Keywords: Aib, 3-aminophenylacetic acid ; NH…N hydrogen bonding ; peptide ; β-sheet
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Crystallographic and spectroscopic studies of a model dipeptide containing unusual amino acid residues establish the presence of an intramolecular, 5-membered NH…N hydrogen bond involving an amide NH (from 3-amino phenyl acetic acid residue) and an amide N atom from an adjacent amino acid residue in solid state and in solution. The dipeptide also forms an infinite β-sheet ribbon structure in crystals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443599
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  • 7
    Electronic Resource
    Electronic Resource
    5-Membered NH...N hydrogen bonded molecular scaffold in a model dipeptide containing 3-aminophenylacetic acid: Crystal and solution conformations (2000)
    Springer
    International journal of peptide research and therapeutics 7 (2000), S. 353-358 
    Details
    ISSN: 1573-3904
    Keywords: Aib ; 3-aminophenylacetic acid ; NH...N hydrogen bonding ; peptide ; β-sheet
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Crystallographic and spectroscopic studies of a model dipeptidecontaining unusual amino acid residues establish the presence ofan intramolecular, 5-membered NH...N hydrogen bond involvingan amide NH (from 3-amino phenyl acetic acid residue) and anamide N atom from an adjacent amino acid residue in solid stateand in solution. The dipeptide also forms an infinite β-sheet ribbon structure in crystals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1013093020585
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  • 8
    Electronic Resource
    Electronic Resource
    Conformational variability of Gly-Gly segments in peptides: A comparison of the crystal structures of an acyclic pentapeptide and an octapeptide (1997)
    New York : Wiley-Blackwell
    Biopolymers 41 (1997), S. 331-336 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The crystal structure of an acyclic pentapeptide, Boc-Gly-Gly-Leu-Aib-Val-OMe, reveals an extended conformation for the Gly-Gly segment, in contrast to the helical conformation determined earlier in the octapeptide Boc-Leu-Aib-Val-Gly-Gly-Leu-Aib-Val-OMe [I. L. Karle, A. Banerjee, S. Bhattacharjya, and P. Balaram [1996] Biopolymers, Vol. 38, pp. 515-526). The pentapeptide crystallizes in space group P21 with one molecule in the asymmetric unit. The cell parameters are: a = 10.979(2) Å, b = 9.625(2) Å, c = 14.141(2) Å, and β = 96.93(1)°, R = 6.7% for 2501 reflections (I 〉 3σ(I)). The Gly-Gly segment is extended (φ1 = -92°, ψ1 = -133°, φ2 = 140°, ψ2 = 170°), while the Leu-Aib segment adopts a type II β-turn conformation (φ3 = -61°, ψ3 = 130°, φ4 = 71°, ψ4 = 6°). The observed conformation for the pentapeptide permits rationalization of a structural transition observed for the octapeptide in solution. An analysis of Gly-Gly segments in peptide crystal structures shows a preference for either β-turn or extended conformations. © 1997 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Ambidextrous molecules: Cylindrical peptide structures formed by fusing left- and right-handed helices (1996)
    New York : Wiley-Blackwell
    Biopolymers 39 (1996), S. 279-285 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: No abstract.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 10
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    Mapping local and global variability in plant trait distributions (2017)
    National Academy of Sciences
    Details
    Publication Date: 2017-12-01
    Description: Our ability to understand and predict the response of ecosystems to a changing environment depends on quantifying vegetation functional diversity. However, representing this diversity at the global scale is challenging. Typically, in Earth system models, characterization of plant diversity has been limited to grouping related species into plant functional types (PFTs), with all trait variation in a PFT collapsed into a single mean value that is applied globally. Using the largest global plant trait database and state of the art Bayesian modeling, we created fine-grained global maps of plant trait distributions that can be applied to Earth system models. Focusing on a set of plant traits closely coupled to photosynthesis and foliar respiration—specific leaf area (SLA) and dry mass-based concentrations of leaf nitrogen (Nm) and phosphorus (Pm), we characterize how traits vary within and among over 50,000 ∼50×50-km cells across the entire vegetated land surface. We do this in several ways—without defining the PFT of each grid cell and using 4 or 14 PFTs; each model’s predictions are evaluated against out-of-sample data. This endeavor advances prior trait mapping by generating global maps that preserve variability across scales by using modern Bayesian spatial statistical modeling in combination with a database over three times larger than that in previous analyses. Our maps reveal that the most diverse grid cells possess trait variability close to the range of global PFT means.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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