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  • 1
    Electronic Resource
    Electronic Resource
    Cyanophenoxy-containing microbial polyesters: Structural analysis, thermal properties, second harmonic generation and in-vivo biodegradability (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Polymer International 39 (1996), S. 205-213 
    Details
    ISSN: 0959-8103
    Keywords: Pseudomonas putida ; poly(β-hydroxyalkanoate) ; microbial polyesters ; poly[3-hydroxy-6(4-cyanophenoxy)hexanoate] ; non-linear optics ; in-vivo biodegradation ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Pseudomonas putida KT 2442 was utilized as biocatalyst to form optoactive poly(β-hydroxyalkanoate)s (PHAs) from a cosubstrate mixture of octanoate and the achiral polarizable carbon source 6(4-cyanophenoxy)hexanoate, CPH. COSY and heteronuclear multiplet quantum correlation experiments were used to assign 1H and 13C NMR signals of 3-hydroxy-6(4-cyanophenoxy)hexanoate (3HCPH) repeat units. The methine carbon of 3HCPH repeat units was sensitive to repeat unit sequence effects, indicating that a substantial fraction of 3HCPH centered triad sequences in the product contain neighboring 3-hydroxyoctanoate and 3-hydroxhexanoate repeat units. Comparing the thermal properties of 0 and 19.6 mol% 3HCPH samples by differential scanning calorimetry shows that 3HCPH incorporation results in melting at temperatures 〉64°C (not seen for the 0 mol% sample), more rapid crystallization and a new Tg transition at ∼ -21°C. These characteristics indicate that chains and/or chain segments are formed that are enriched in 3HCPH which phaseseparate and form a unique crystal structure. Measurements of second harmonic generation (SHG) intensities carried out using in-situ corona-poled samples showed weak SHG signals that increased by a factor of 8 for an increase in the 3HCPH content from 26 to 34 mol%. Comparatively higher SHG intensities (5 times) were found for PHAs which contained 5.1 mol% 3-hydroxy-6(4-nitrophenoxy)hexanoate (3HNPH) repeat units relative to a PHA with 17 mol% 3HCPH. In-vivo biodegradation studies of microbial polyesters prepared with and without 3HCPH repeat units showed that PHA chains with 3HCPH degraded to lesser extents (weight loss of ∼ 20 and 50% over 72 h incubations). The large increase in polydispersity from 1.9 to 4.3 observed during in-vivo biodegradation of microbial polyesters containing 3HCPH repeat units was attributed to the existence of chains with highly variable contents of 3HCPH repeat units.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 2
    Electronic Resource
    Electronic Resource
    Editorial (1995)
    New York : Wiley-Blackwell
    Biopolymers 37 (1995), S. 176-176 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360370302
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  • 3
    Electronic Resource
    Electronic Resource
    A review of the utility of soluble peptide combinatorial libraries (1995)
    New York : Wiley-Blackwell
    Biopolymers 37 (1995), S. 221-240 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: This is paper reviews the preparation and use of soluble synthetic combinatorial libraries (SCLs) made up of millions of peptide and nonpeptide sequences for the identification of highly active individual compounds. First presented in 1991. SCLs have been prepared in a number of different lengths and formats, and are composed entirely of L-, D-, and unnatural amino acids. Also, existing peptide libraries have been chemically transformed to yield large diversities of nonpeptidic compounds. This review encompasses the published work from this laboratory using SCLs for the identification of antigenic sequences recognized by monoclonal antibodies, novel peptide agonists and antagonists to opioid receptors, new trypsin inhibitors, novel antibacterials, and compounds that inhibit melittin's hemolytic activity. SCLs offer a fundamental, practical advance in the study of interactions between peptide and nonpeptide sequences and their biochemical or pharmacological targets. © 1994 John Wiley & Sons, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360370306
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  • 4
    Electronic Resource
    Electronic Resource
    Poly(p-Phenylenebenzobisoxazole) fiber with polyphenylene sulfide pendent groups (1995)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 33 (1995), S. 159-164 
    Details
    ISSN: 0887-624X
    Keywords: poly(p-phenylenebenzobisoxazole) ; polyphenylene sulfide ; pendent group ; crosslinking ; heat treatment ; compressive strength ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Poly(p-phenylenebenzobisoxazole) (PBO) fiber with polyphenylene sulfide (PPS) pendent groups was made to improve PBO fiber compressive strength by crosslinking. PPS moieties allowed the polymeric network to crosslink at heat-treatment temperatures at which PBO does not thermally degrade. PBO-PPS fiber heat-treated for 30 s at 600°C did not dissolve or break up in methanesulfonic acid. Compressive strength of crosslinked fiber was about 20% better than that of unmodified PBO fiber. In another experiment, 10 mol % of 2,5-diphenylsulfideterephthalic acid was incorporated into PBO fiber. The side chain of one phenyl sulfide unit was too short to enhance crosslinking, and the fiber had about the same compressive strength as unmodified PBO fiber. © 1995 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pola.1995.080330118
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  • 5
    Electronic Resource
    Electronic Resource
    Retardation of dibenzo polyether-formaldehyde resin formation by alkali-metal cations (1995)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 33 (1995), S. 2267-2274 
    Details
    ISSN: 0887-624X
    Keywords: dibenzo polyether ; formaldehyde condensation polymerization ; alkali-metal cation sorption ; template polymerization ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Macrocyclic polyethers are well-known complexing agents for alkali-metal and alkaline earth-metal cations. The influence of alkali-metal cations upon the polycondensation rate of acyclic and cyclic dibenzo polyethers with formaldehyde in formic acid and alkali-metal cation sorption by some of the resultant resins have been investigated. For certain dibenzo polyether and alkali-metal cation combinations, polymer formation is markedly reduced. The alkali-metal cation that provides the best fit for the macrocyclic polyether cavity produces the greatest retardation of polymer formation. It is proposed that metal ion complexation renders the dibenzo polyether monomer inert to polymerization under the reaction conditions. No template effect for alkali-metal cation sorption by dibenzo polyether carboxylic acid resins was observed. © 1995 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pola.1995.080331321
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  • 6
    Electronic Resource
    Electronic Resource
    New polymer electrolyte nanocomposites: Melt intercalation of poly(ethylene oxide) in mica-type silicatesThis work was sponsored in part by Corning, Inc., and by generous gifts from Xerox and Southern Clay Products. RAV is supported by a DoD Fellowship. We benefitted from the use of MRL Central Facilities funded by the National Science Foundation. (1995)
    Weinheim : Wiley-Blackwell
    Advanced Materials 7 (1995), S. 154-156 
    Details
    ISSN: 0935-9648
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/adma.19950070210
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  • 7
    Electronic Resource
    Electronic Resource
    Electroluminescent properties of self-assembled polymer thin filmsThis work was supported by the New Jersey Commission of Science and Technology through the Advanced Technology Center for Photonic and Optoelectronic Materials (ATC/POEM), as well as the Princeton Materials Institute (PMI), the National Science Foundation MRL Program (DMR-91-20668, TMS and MJM). (1995)
    Weinheim : Wiley-Blackwell
    Advanced Materials 7 (1995), S. 395-398 
    Details
    ISSN: 0935-9648
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/adma.19950070411
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  • 8
    Electronic Resource
    Electronic Resource
    Flow-injection liposome immunoanalysis (FILIA) with electrochemical detection (1995)
    Weinheim : Wiley-Blackwell
    Electroanalysis 7 (1995), S. 838-845 
    Details
    ISSN: 1040-0397
    Keywords: Liposomes ; Immunoanalysis ; Alachlor ; Flow-injection analysis ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An automated flow-injection liposome immunoanalysis (FILIA) system with electrochemical detection has been developed to measure the herbicide alachlor. The computer-controlled system is composed of commercially available components, with the exception of the reusable immunoreactor column packing material (glass beads) which is covalently coated with antibody specific for the analyte of interest. Use of such components affords full automation while simplifying the construction of, and modifications to, the system. The assay is based on competition in the immunoreactor column between alachlor-tagged liposomes containing an electroactive marker, ferrocyanide, and free alachlor, with quantitative signal amplification provided by lysis of bound liposomes with surfactant to release the marker. An optimized assay permits the detection of 0.5 ng alachlor in a spiked water sample. The electrochemical detector is operated in the controlled-potential, amperometric mode in which ferrocyanide is oxidized at low potential (+ 0.330 V vs. Ag/AgCl), thus minimizing electroactive interferences. The relationships among the various operational parameters (e.g., potential, flow rate, assay time, composition of solutions) are discussed, and the optimization of these parameters is presented.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elan.1140070909
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  • 9
    Electronic Resource
    Electronic Resource
    The foldability landscape of model proteins (1997)
    New York : Wiley-Blackwell
    Biopolymers 42 (1997), S. 427-438 
    Details
    ISSN: 0006-3525
    Keywords: protein folding ; molecular evolution ; lattice models ; fitness landscapes ; spin glasses ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Molecular evolution may be considered as a walk in a multidimensional fitness landscape, where the fitness at each point is associated with features such as the function, stability, and survivability of these molecules. We present a simple model for the evolution of protein sequences on a landscape with a precisely defined fitness function. We use simple lattice models to represent protein structures, with the ability of a protein sequence to fold into the structure with lowest energy, quantified as the foldability, representing the fitness of the sequence. The foldability of the sequence is characterized based on the spin glass model of protein folding. We consider evolution as a walk in this foldability landscape and study the nature of the landscape and the resulting dynamics. Selective pressure is explicitly included in this model in the form of a minimum foldability requirement. We find that different native structures are not evenly distributed in interaction space, with similar structures and structures with similar optimal foldabilities clustered together. Evolving proteins marginally fulfill the selective criteria of foldability. As the selective pressure is increased, evolutionary trajectories become increasingly confined to “neutral networks,” where the sequence and the interactions can be significantly changed while a constant structure is maintained. © 1997 John Wiley & Sons, Inc. Biopoly 42: 427-438, 1997
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Secondary structure induction in aqueous vs membrane-like environments (1997)
    New York : Wiley-Blackwell
    Biopolymers 42 (1997), S. 489-498 
    Details
    ISSN: 0006-3525
    Keywords: amino acid propensity ; secondary structure ; aqueous environments ; membrane-like environments ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational propensity of the 20 naturally occurring amino acids was determined in aqueous 3-[N-morpholino]propane-sulfonic acid (MOPS) buffer, protein interior-like [nonmicellar sodium dodecylsulfate (SDS)] and membrane-like environments (micellar SDS and lysophosphatidylglycerol/lysophosphatidylcholine micelles) using a single “guest” position in a polyalanine-based model host peptide (Ac-KYA13K-NH2). This model system allows the intrinsic α-helical or β-sheet propensity of the amino acids to be determined without intra- and interchain side chain interactions. The overall environment dependence observed for the conformational propensity for the amino acids studied confirms the importance of determining propensity in lipidic environments to better elucidate the biological functions of proteins. The hydrophobic interactions between peptide side chains and lipids appeared to be the primary forces driving the conformational induction in lipidic environments of the model peptides studied. Finally, when comparing the results of these studies with those reported in the literature, the local environment was found to highly influence 65% of the 20 naturally occurring amino acids. © 1997 John Wiley & Sons, Inc. Biopoly 42: 489-498, 1997
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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