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  • 2000-2004  (42)
  • 1975-1979  (17)
  • 1
    Electronic Resource
    Electronic Resource
    Solid State Conformation of Poly-N 5-(3-hydroxypropyl)-L-glutamine by X Rays (1977)
    s.l. : American Chemical Society
    Macromolecules 10 (1977), S. 715-716 
    Details
    ISSN: 1520-5835
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ma60057a047
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  • 2
    Electronic Resource
    Electronic Resource
    Conformational Properties of Poly(L-azetidine-2-carboxylic acid) in Solution as Studied by Carbon-13 and Proton Nuclear Magnetic Resonance Spectroscopy (1975)
    s.l. : American Chemical Society
    Macromolecules 8 (1975), S. 140-145 
    Details
    ISSN: 1520-5835
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ma60044a010
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  • 3
    Electronic Resource
    Electronic Resource
    Free Amino Acid Profiles During Ripening of Port Salut Argentino Cheese After Frozen Storage (2002)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 67 (2002), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Free amino acid profiles of Port Salut Argentino cheeses at different storage conditions (ripening with and without previous frozen storage), ripening times (1, 6, 13, 27, and 56 d), and cheese zones (central and external) were studied. Derivatization with o-phtaldialdehyde and a C18 column were used for chromatographic separations. Principal component analysis reduced data to 2 dimensions where unripened cheeses (1 to 13 d) were grouped independently of ripening time, sampling zone, and storage condition. Ripened cheeses (27 and 56 d) showed scattering according to ripening time. The contribution of free amino acid profiles to quality in cheeses preserved by frozen storage may be considered similar to that in traditionally ripened cheeses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2002.tb09576.x
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  • 4
    Electronic Resource
    Electronic Resource
    Texture Changes During the Ripening of Port Salut Argentino Cheese in 2 Sampling Zones (2002)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 67 (2002), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Texture changes during ripening of Port Salut Argentino cheese for different sampling zones were studied. Compression relaxation tests were performed and results were analyzed using both Maxwellian and Peleg's models. Elastic equilibrium modulus obtained from the Maxwellian model decreased from 1.22 to 0.11 104Pa during ripening. The constants derived from Peleg's model, k1 and k2, diminished with ripening time from 1.18 to 0.71 min and from 1.27 to 1.12, respectively. Asymptotic equilibrium modulus from Peleg's model decreased from 0.95 to 0.07 104Pa during ripening. Rate parameters derived from a 1st order kinetics applied to both equilibrium moduli showed that the decrease was faster in the external zone (0.0846 d−1) than in the central zone (0.0368 d−1). The correlation between equilibrium moduli, salt concentration, moisture content, and maturation indexes was obtained with a determination coefficient of 0.76.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2002.tb08727.x
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  • 5
    Electronic Resource
    Electronic Resource
    Effect of Frozen Storage Time on the Proteolysis of Soft Cheeses Studied by Principal Component Analysis of Proteolytic Profiles (2002)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 67 (2002), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : Port Salut Argentino cheeses were frozen, stored in a freezer at −22 °C for different periods, and slowly thawed. After thawing, some cheeses were immediately sampled while others were sampled after different refrigerated storage times. Reversed Phase High Performance Liquid chromatograms were compared applying principal component analysis. The information obtained from the chromatograms was successfully summarized in 2 dimensions accounting for 93.4% of the data variation. According to sample grouping, there were differences between Port Salut Argentino cheeses due to the ripening during refrigerated storage for up to 60 days at 4 7deg;C. However, for cheeses that were sampled immediately after slow thawing, there was no significant effect of the frozen storage time in cheese proteolysis, from 1 to 60 d.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2002.tb09436.x
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  • 6
    Electronic Resource
    Electronic Resource
    Bildung, Eigenschaften und Strukturen von Bis(o-hydroxybenzylidenamin) (1976)
    Springer
    Colloid & polymer science 254 (1976), S. 769-769 
    Details
    ISSN: 1435-1536
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01643927
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  • 7
    Electronic Resource
    Electronic Resource
    Synthesis of sequential polypeptides containing L-azetidine-2-carboxylic acid residues (1975)
    New York : Wiley-Blackwell
    Biopolymers 14 (1975), S. 2211-2230 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The synthesis and characterization of a series of sequential polypeptides with the repeating sequences Aze-Pro-Aze, Pro-Aze-Pro, Pro-Aze-Gly, Aze-Pro-Gly, Ala-Aze-Gly, Aze-Ala-Gly, and Pro-Pro-Gly are reported. The polymers were prepared by the active ester method, using the p-nitrophenyl, pentachlorophenyl, and N-hydroxysuccinimide esters as the polymerizable tripeptide derivatives. Except for poly(Ala-Aze-Gly) obtained via the N-hydroxysuccinimide ester, all polymers were isolated in good yields and have weight-average molecular weights in the range 10,000-30,000. The molecular weights have been determined by applying the calibrated gel chromatography system described by Fairweather et al. [J. Chromatogr. (1972) 67, 157] and by viscometry. All di- and tripeptide intermediates were chemically and optically pure.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1975.360141016
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  • 8
    Electronic Resource
    Electronic Resource
    Conformational properties of the sequential polyproline analogs poly(Pro-Aze-Pro) and poly(Aze-Pro-Aze) (1976)
    New York : Wiley-Blackwell
    Biopolymers 15 (1976), S. 1233-1242 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The lack of the positive band at around 226 nm in the CD spectra of poly(prolyl-azetidine-2-carbonyl-proline) in trifluoroethanol and of poly(azetidine-2-carbonyl-prolyl-azetidine-2-carboxylic) acid in F3EtOH and water, the hyperchromism of the absorption maximum at about 202 nm, and the extremely small intensity of the Cβ-Pro, Cγ-Pro, and Cβ-Aze signals for the cis peptide bonds in the 13C nmr spectrum of poly(Pro-Aze-Pro) in F3EtOH indicate that both polyproline analogs exist as disordered chains in this solvent, the trans peptide group being maintained. The disordering of the chains is attributed to an increase in the accessible range of ψ due to the reduced dimensions of the square ring of L-azetidine-2-carboxylic acid residue relative to the pyrrolidine ring of proline and to strong interactions of the haloalcohol with the peptide groups of the chains.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1976.360150702
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  • 9
    Electronic Resource
    Electronic Resource
    Conformational studies on the pyridoxal Schiff bases of polypeptides (1978)
    New York : Wiley-Blackwell
    Biopolymers 17 (1978), S. 897-908 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The pyridoxal Schiff bases of the polypeptides poly(L-lysine), poly(L-ornithine), and poly(L-α,γ-diaminobutyric acid) were prepared and investigated in water/methanol by CD spectra and equilibrium dialysis experiments. Only the poly(L-α,γ-diaminobutyric acid) derivative is characterized by a relevant optical activity similar to that found in pyridoxal enzymes. The stereospecific interactions between the pyridoxylideneimine group and the polypeptide chain prevent the hydrolysis reaction of the aldimine bond.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1978.360170408
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  • 10
    Electronic Resource
    Electronic Resource
    Solution conformations of some azetidine cyclic peptidesThis is paper xxi of the series “Cyclic Peptides.” Paper XX of this series (Boni et al.) (1978)
    New York : Wiley-Blackwell
    Biopolymers 17 (1978), S. 2401-2413 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The 1H-nmr spectra (270 MHz) of cyclic di- and tri-L-azatidine-2-carboxylic acid [cy-clo(L-Aze)2 and cyclo(L-Aze)3] were determined in CDCl3 and D2O and computer simulated. The spectral results were compared with those obtained with cyclo (L-Pro)2 and cyclo (L,-Pro)3. In CDCl3 and D2O solution, the four membered ring of cyclo (L-Aze)2 is puckered with the α-proton in a pseudo-axial position, and the φ angle is smaller in absolute value than -60°, as found for cyclo (L-Pro)2,. The puckering of the four-membered ring of cyclo(L,-Aze)3 in CDCl3 has the α-proton in a pseudo-equatorial position and φ angle larger in absolute value than -60°, in agreement with cyclo(L-Pro)3. In D2O, cyclo(L-Aze)3 was found to interconvert rapidly between different conformers. In the azetidine cyclic peptides studied, the range of values found for the φ angles was smaller than in the related proline cyclic peptides, indicating greater rigidity in the four-membered ring.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1978.360171009
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