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  • Chemistry  (7,254)
  • Chemical Engineering  (658)
  • Biochemistry and Biotechnology  (457)
  • 1985-1989  (7,254)
  • 1985  (7,254)
Collection
Keywords
Publisher
Years
  • 1985-1989  (7,254)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Obituary (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985), S. vi 
    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.360240102
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular model for the complex between Concanavalin A and a biantennary-complex class glycopeptide (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985), S. 49-63 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A molecular model for the complex formed between the jack bean lectin concanavalin A (Con A) and glycopeptides of the complex biantennary class is described. The model was derived using coordinates for Con A determined by x-ray crystalographic refinement techniques, with 1.75-Å resolution data, and coordinates for the glycopeptides obtained from 1H-nmr measurements, using the nuclear Overhauser effect. Previous solution and crystallographic studies provided several constraints on the possible mode of interaction of the lectin and the glycopeptide. Examination of the model suggests that the glycopeptide binding site is defined by four loops on the protein surface made up by amino acid residues: 12-18, 98-102, 205-208, and 226-229. Within these loops, it favorable interactions with high-affinity ligands and tose responsible for the unfavourable interactions with poor ligands.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360240106
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  • 3
    Electronic Resource
    Electronic Resource
    Transfer of peptide hormones from aqueous to membrane phasesWe take great pleasure in dedicating this manuscript to Professor Elkan R. Blout on the occasion of his sixty-fifty birthday. (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985), S. 105-116 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Peptide hormones and neurotransmitters are functional amphiphilic substances that deploy their chared and nonpolar substituents as required for traversing aqueous phases en rout to their ultimate transfer into the lipid-rich environment of their membrane-embedded receptors. As a means of determining the role(s)that cellular membrane lipids may play in mediating these events, we describe an experimental approach, using high-resolution 1H-and 13C-nmr spectroscopy, for delineation of the structures of complexes between the (neurotransmitter pentapeptide) enkephalins and micellar and vesicular phospholipid particles. Residue-specific enkephalin interactions with lipid are identified; affinity constants for the hydrophobic component(s) of peptide/lipid association are calculated for enkephalin and several of its analogs; and comparisons with morphine are presented. Finally, based on molecular details obtained from nmr experiments, a model is proposed for the encoutner of a peptide hormone with a phospholipid membrane surface.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360240110
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  • 4
    Electronic Resource
    Electronic Resource
    Masthead (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985) 
    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.360240201
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  • 5
    Electronic Resource
    Electronic Resource
    The octamers d(CGCGCGCG) and d(CGCATGCG) both crystallize as Z-DNA in the same hexagonal lattice (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985), S. 243-250 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Both (dC-dG)4 and d(CGCATGCG) crystallize in hexagonal lattices and their three-dimensional structure has been solved by x-ray diffraction analysis. Both molecules are found to form Z-DNA, although the fine details of the structure cannot be visualized due to the statistical disordering of the molecules along the c-axis, which is brought about by the symmetry constraints of the space group. This represents the first time in which the unmodified dinucleotide sequences CpAp and TpGp have been found to form Z-DNA in a crystalline lattice.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360240118
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  • 6
    Electronic Resource
    Electronic Resource
    Electron microscopy of the melting of sequenced DNA (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985), S. 359-377 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Differential melting curves (DMCs) of DNAs pA03 and pBR322 in solutions of different ionic strength (0.02 and 0.2M Na+) were obtained. A previously developed procedure of glyxal fixation of partially denatured DNA molecules at temperatures within the melting range was used to construct electron-microscopic melting maps for pBR322 and pAO3 plasmid DNA and for the replicative form of bacteriophage φX174 DNA, allowing the melting of these DNA molecules to be followed in solutions of low (0.1 × SSC) and high (1 × SSC) ionic strength. In spite of the fact that the melting was at nonequilibrium at the low ionic strength, the melting maps for the two kinds of solutions practically coincided. Experimental data are compared with theoretical calculations based on the Fixman-Freire algorithm. The conclusion is that the melting pattern of these DNAs is, on the whole, correctly described by the theory, although there are appreciable differences between the theoretical and experimental differential melting curves. We have also determined the relation between the melting temperature of a region and its GC content, with allowances made for the boundary conditions of melting in 0.1 × SSC and 1 × SSC solutions, and have analyzed the theoretical shape of peaks of the DMCs.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360240205
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  • 7
    Electronic Resource
    Electronic Resource
    A highly crystalline cellulose from Rhizoclonium hieroglyphicum (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985), S. 421-423 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360240209
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  • 8
    Electronic Resource
    Electronic Resource
    Masthead (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985) 
    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.360240301
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  • 9
    Electronic Resource
    Electronic Resource
    Dielectric effects in biopolymers: The theory of ionic saturation revisited (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985), S. 427-439 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Electrostatic effects are believed to determine the molecular structure and function of macromolecules in many ways. In metallo-based enzymes and in metal-macromolecule interactions in solution, these effects may predominate. In order to tackle metal ion-nucleic acid interactions theoretically, we propose a modification of Debye's distance-dependent dielectric function first proposed more than 50 years ago. This function more closely approximates physical reality at small interatomic separations. Our theory yields a dielectric function that gives reasonable agreement with experimental data in preliminary calculations.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360240302
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  • 10
    Electronic Resource
    Electronic Resource
    A simple and novel interpretation of the three-dimensional structure of globular proteins based on quantum-mechanical computations on small model molecules. I (1985)
    New York : Wiley-Blackwell
    Biopolymers 24 (1985), S. 491-508 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: It is suggested that the three-dimensional structure of globular proteins is partly determined by a framework of strengthened hydrogen bonds that involves both ionic side chains and water molecules in addition to the polypeptide backbone. This conclusion follows from a combination of the results of ab initio molecular-orbital computations on small model molecules and high-accuracy x-ray data on the rubredoxin molecule. The computations yield the idea of hydrogen-bonded bridges that are built from tens of atoms, and the experimental information yields the idea that the bridges are assembled into clusters, each of which is built from hundreds of atoms. Some 10 such clusters then form a globular protein.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360240306
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